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Conserved domains on  [gi|397529548|ref|NP_001257588|]
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serine--pyruvate aminotransferase isoform 2 [Rattus norvegicus]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 56-180 2.98e-47

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member cd06451:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 356  Bit Score: 157.84  E-value: 2.98e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548  56 HHTLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKdPEIRLPTITTVTVPAGYNWRDIVSYVL 135
Cdd:cd06451  234 PHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAK-PELRSPTVTAVLVPEGVDGDEVVRRLM 312

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 397529548 136 DHFNIEISGGLGPSEDKVLRIGLLGYnATTENADRVAEALREALQ 180
Cdd:cd06451  313 KRYNIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
 
Name Accession Description Interval E-value
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 56-180 2.98e-47

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 157.84  E-value: 2.98e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548  56 HHTLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKdPEIRLPTITTVTVPAGYNWRDIVSYVL 135
Cdd:cd06451  234 PHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAK-PELRSPTVTAVLVPEGVDGDEVVRRLM 312

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 397529548 136 DHFNIEISGGLGPSEDKVLRIGLLGYnATTENADRVAEALREALQ 180
Cdd:cd06451  313 KRYNIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 56-180 1.51e-39

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 137.91  E-value: 1.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548  56 HHTLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKDpEIRLPTITTVTVPAGYNWRDIVSYVL 135
Cdd:COG0075  233 PYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEE-EYRSPTVTAVRVPEGVDAAALRKRLK 311

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 397529548 136 DHFNIEISGGLGPSEDKVLRIGLLGYNaTTENADRVAEALREALQ 180
Cdd:COG0075  312 ERYGIEIAGGLGPLKGKIFRIGHMGYV-NPEDVLRTLAALEEALR 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 57-163 6.96e-30

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 112.93  E-value: 6.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548  57 HTLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKDPEIRLPTITTVTVPAGYNWRDIVSYVLD 136
Cdd:PLN02409 249 YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVPEGIDSAEIVKNAWK 328

                         90       100
                 ....*....|....*....|....*..
gi 397529548 137 HFNIEISGGLGPSEDKVLRIGLLGYNA 163
Cdd:PLN02409 329 KYNLSLGLGLNKVAGKVFRIGHLGNVN 355
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 58-171 1.13e-13

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 68.04  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548   58 TLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKDPeiRLPTITTVTVPaGYNWRDIVSYvLDH 137
Cdd:pfam00266 252 TPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNFK-GVHPHDVATL-LDE 327

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 397529548  138 FNIEISGGL---GPSED-----KVLRIGLLGYNaTTENADRV 171
Cdd:pfam00266 328 SGIAVRSGHhcaQPLMVrlglgGTVRASFYIYN-TQEDVDRL 368
 
Name Accession Description Interval E-value
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 56-180 2.98e-47

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 157.84  E-value: 2.98e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548  56 HHTLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKdPEIRLPTITTVTVPAGYNWRDIVSYVL 135
Cdd:cd06451  234 PHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAK-PELRSPTVTAVLVPEGVDGDEVVRRLM 312

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 397529548 136 DHFNIEISGGLGPSEDKVLRIGLLGYnATTENADRVAEALREALQ 180
Cdd:cd06451  313 KRYNIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 56-180 1.51e-39

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 137.91  E-value: 1.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548  56 HHTLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKDpEIRLPTITTVTVPAGYNWRDIVSYVL 135
Cdd:COG0075  233 PYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEE-EYRSPTVTAVRVPEGVDAAALRKRLK 311

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 397529548 136 DHFNIEISGGLGPSEDKVLRIGLLGYNaTTENADRVAEALREALQ 180
Cdd:COG0075  312 ERYGIEIAGGLGPLKGKIFRIGHMGYV-NPEDVLRTLAALEEALR 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 57-163 6.96e-30

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 112.93  E-value: 6.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548  57 HTLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKDPEIRLPTITTVTVPAGYNWRDIVSYVLD 136
Cdd:PLN02409 249 YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVPEGIDSAEIVKNAWK 328

                         90       100
                 ....*....|....*....|....*..
gi 397529548 137 HFNIEISGGLGPSEDKVLRIGLLGYNA 163
Cdd:PLN02409 329 KYNLSLGLGLNKVAGKVFRIGHLGNVN 355
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 58-171 1.13e-13

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 68.04  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548   58 TLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKDPeiRLPTITTVTVPaGYNWRDIVSYvLDH 137
Cdd:pfam00266 252 TPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNFK-GVHPHDVATL-LDE 327

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 397529548  138 FNIEISGGL---GPSED-----KVLRIGLLGYNaTTENADRV 171
Cdd:pfam00266 328 SGIAVRSGHhcaQPLMVrlglgGTVRASFYIYN-TQEDVDRL 368
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
67-181 6.46e-05

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 42.43  E-value: 6.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529548  67 LRESLALISEQGLENSWRRHREATAHLHKCLREL-GLKFF-VKDPEIRLPtITTVTVpAGYNWRDIVSYvLDHFNIEISG 144
Cdd:COG0520  276 LGAAIDYLEAIGMEAIEARERELTAYALEGLAAIpGVRILgPADPEDRSG-IVSFNV-DGVHPHDVAAL-LDDEGIAVRA 352

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 397529548 145 GLGPSEDKVLRIGLLG--------YNaTTENADRVAEALREALQH 181
Cdd:COG0520  353 GHHCAQPLMRRLGVPGtvrasfhlYN-TEEEIDRLVEALKKLAEL 396
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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