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Conserved domains on  [gi|1532591145|ref|WP_125121509|]
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aminotransferase class V-fold PLP-dependent enzyme, partial [Bacillus subtilis]

Protein Classification

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme( domain architecture ID 1001916)

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme similar to Staphylococcus aureus orn/lys/arg decarboxylase family protein

CATH:  3.90.105.10|3.40.640.10|3.90.1150.150
Gene Ontology:  GO:0016831
PubMed:  25615531|10800595|35697072

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LdcC super family cl34388
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
1-137 5.74e-81

Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];


The actual alignment was detected with superfamily member COG1982:

Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 246.18  E-value: 5.74e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYGIAHGITASAVERALELHPDTKAVLVINPTYFGVA 80
Cdd:COG1982    97 AMILAVCGPGDKVLVPRNCHKSVIHGLILSGAIPVYLNPEIDNELGIIGGITPEAVEEALIEHPDAKAVLITNPTYYGVC 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1532591145  81 GDLERIVAVAHAQDVPVLVDEAHGVHLPFHDELPLSAMQAGADVAATSVHKLGGSMT 137
Cdd:COG1982   177 YDLKAIAELAHEHGIPVLVDEAHGAHFGFHPDLPRSAMEAGADLVVQSTHKTLGALT 233
 
Name Accession Description Interval E-value
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
1-137 5.74e-81

Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 246.18  E-value: 5.74e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYGIAHGITASAVERALELHPDTKAVLVINPTYFGVA 80
Cdd:COG1982    97 AMILAVCGPGDKVLVPRNCHKSVIHGLILSGAIPVYLNPEIDNELGIIGGITPEAVEEALIEHPDAKAVLITNPTYYGVC 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1532591145  81 GDLERIVAVAHAQDVPVLVDEAHGVHLPFHDELPLSAMQAGADVAATSVHKLGGSMT 137
Cdd:COG1982   177 YDLKAIAELAHEHGIPVLVDEAHGAHFGFHPDLPRSAMEAGADLVVQSTHKTLGALT 233
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 1-137 1.45e-62

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 193.23  E-value: 1.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYGIAHGITASAVERALELHPDTKAVLVINPTYFGVA 80
Cdd:cd00615    90 AVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYGIAGGIPPETFKKALIEHPDAKAAVITNPTYYGIC 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1532591145  81 GDLERIVAVAHAQDVPVLVDEAHGVHLPFHDELPLSAMQAGADVAATSVHKLGGSMT 137
Cdd:cd00615   170 YNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSSAAMAGADIVVQSTHKTLPALT 226
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
1-137 1.08e-39

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 137.25  E-value: 1.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEyDETYGIAHGITASA-----VERALELHPDTKA---VLVI 72
Cdd:pfam01276  97 TVGMAVCTPGDTILIDRNCHKSIHHALMLSGATPVYLEPS-RNAYGIIGGIPLHEfqeetLKEAIAEVPDAKGprlAVIT 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1532591145  73 NPTYFGVAGDLERIVAVAHAQDVPVLVDEAHGVHLPFHdELPLSAMQAGAD-------VAATSVHKLGGSMT 137
Cdd:pfam01276 176 NPTYDGVLYNAKEIVDTLHHLSDPILFDSAWVGYEQFI-PIYADASPMGGEnengpgiFVTQSVHKLLAALS 246
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 1-105 9.82e-09

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 52.15  E-value: 9.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVF--IHPE---YDETyGIAHGITasaveralelhPDTKAVLVINpt 75
Cdd:PRK11706   62 AALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFvdIRPDtmnIDET-LIEAAIT-----------PKTRAIVPVH-- 127

                          90       100       110
                  ....*....|....*....|....*....|
gi 1532591145  76 YFGVAGDLERIVAVAHAQDVPVLVDEAHGV 105
Cdd:PRK11706  128 YAGVACEMDTIMALAKKHNLFVVEDAAQGV 157
 
Name Accession Description Interval E-value
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
1-137 5.74e-81

Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 246.18  E-value: 5.74e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYGIAHGITASAVERALELHPDTKAVLVINPTYFGVA 80
Cdd:COG1982    97 AMILAVCGPGDKVLVPRNCHKSVIHGLILSGAIPVYLNPEIDNELGIIGGITPEAVEEALIEHPDAKAVLITNPTYYGVC 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1532591145  81 GDLERIVAVAHAQDVPVLVDEAHGVHLPFHDELPLSAMQAGADVAATSVHKLGGSMT 137
Cdd:COG1982   177 YDLKAIAELAHEHGIPVLVDEAHGAHFGFHPDLPRSAMEAGADLVVQSTHKTLGALT 233
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 1-137 1.45e-62

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 193.23  E-value: 1.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYGIAHGITASAVERALELHPDTKAVLVINPTYFGVA 80
Cdd:cd00615    90 AVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYGIAGGIPPETFKKALIEHPDAKAAVITNPTYYGIC 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1532591145  81 GDLERIVAVAHAQDVPVLVDEAHGVHLPFHDELPLSAMQAGADVAATSVHKLGGSMT 137
Cdd:cd00615   170 YNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSSAAMAGADIVVQSTHKTLPALT 226
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
1-137 1.08e-39

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 137.25  E-value: 1.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEyDETYGIAHGITASA-----VERALELHPDTKA---VLVI 72
Cdd:pfam01276  97 TVGMAVCTPGDTILIDRNCHKSIHHALMLSGATPVYLEPS-RNAYGIIGGIPLHEfqeetLKEAIAEVPDAKGprlAVIT 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1532591145  73 NPTYFGVAGDLERIVAVAHAQDVPVLVDEAHGVHLPFHdELPLSAMQAGAD-------VAATSVHKLGGSMT 137
Cdd:pfam01276 176 NPTYDGVLYNAKEIVDTLHHLSDPILFDSAWVGYEQFI-PIYADASPMGGEnengpgiFVTQSVHKLLAALS 246
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 7-105 2.01e-10

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 56.78  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   7 VGPNEKIIVPRNVHKSVMSALVLTGAHPVF--IHPEydeTYGIahgiTASAVERALElhPDTKAVLVINptYFGVAGDLE 84
Cdd:cd00616    55 IGPGDEVIVPSFTFVATANAILLLGATPVFvdIDPD---TYNI----DPELIEAAIT--PRTKAIIPVH--LYGNPADMD 123

                          90       100
                  ....*....|....*....|.
gi 1532591145  85 RIVAVAHAQDVPVLVDEAHGV 105
Cdd:cd00616   124 AIMAIAKRHGLPVIEDAAQAL 144
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 7-130 1.20e-09

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 54.60  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   7 VGPNEKIIVPRNVHKSVMSALVLTGAHPVF--IHPEYdetygiaHGITASAVERALElhPDTKAVLVINptYFGVAGDLE 84
Cdd:pfam01041  61 VGPGDEVITPSFTFVATANAALRLGAKPVFvdIDPDT-------YNIDPEAIEAAIT--PRTKAIIPVH--LYGQPADMD 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1532591145  85 RIVAVAHAQDVPVLVDEAHGVHLPFHDElplsAMQAGADVAATSVH 130
Cdd:pfam01041 130 AIRAIAARHGLPVIEDAAHALGATYQGK----KVGTLGDAATFSFH 171
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
7-104 5.99e-09

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 52.76  E-value: 5.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   7 VGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDeTYGIahgiTASAVERALElhPDTKAVLVINptYFGVAGDLERI 86
Cdd:COG0399    67 IGPGDEVITPAFTFVATANAILYVGATPVFVDIDPD-TYNI----DPEALEAAIT--PRTKAIIPVH--LYGQPADMDAI 137

                          90       100
                  ....*....|....*....|
gi 1532591145  87 VAVAHAQDVPVLVD--EAHG 104
Cdd:COG0399   138 MAIAKKHGLKVIEDaaQALG 157
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 1-105 9.82e-09

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 52.15  E-value: 9.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVF--IHPE---YDETyGIAHGITasaveralelhPDTKAVLVINpt 75
Cdd:PRK11706   62 AALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFvdIRPDtmnIDET-LIEAAIT-----------PKTRAIVPVH-- 127

                          90       100       110
                  ....*....|....*....|....*....|
gi 1532591145  76 YFGVAGDLERIVAVAHAQDVPVLVDEAHGV 105
Cdd:PRK11706  128 YAGVACEMDTIMALAKKHNLFVVEDAAQGV 157
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
2-105 1.00e-07

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 49.25  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   2 MIMGVvGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYgiahgITASAVERALElhPDTKAVLVINptYFGVAG 81
Cdd:PRK11658   66 MALGI-GPGDEVITPSLTWVSTLNMIVLLGATPVMVDVDRDTLM-----VTPEAIEAAIT--PRTKAIIPVH--YAGAPA 135

                          90       100
                  ....*....|....*....|....
gi 1532591145  82 DLERIVAVAHAQDVPVLVDEAHGV 105
Cdd:PRK11658  136 DLDAIRAIGERYGIPVIEDAAHAV 159
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 3-119 3.08e-07

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 47.82  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   3 IMGVVGPNEKIIVPR---NVHKSvmsALVLTGAHPVFIHPEYDETYGIahgiTASAVERALElhPDTKAVLVI---NPTy 76
Cdd:COG0436   107 LLALLNPGDEVLVPDpgyPSYRA---AVRLAGGKPVPVPLDEENGFLP----DPEALEAAIT--PRTKAIVLNspnNPT- 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1532591145  77 fGV---AGDLERIVAVAHAQDVPVLVDEAHGvHLPFHDELPLSAMQ 119
Cdd:COG0436   177 -GAvysREELEALAELAREHDLLVISDEIYE-ELVYDGAEHVSILS 220
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 1-123 3.96e-07

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 47.72  E-value: 3.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYGIahgitaSAVERALELHPDTKAVLVI---NPTyf 77
Cdd:cd00609    74 LLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLL------DLELLEAAKTPKTKLLYLNnpnNPT-- 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1532591145  78 GV---AGDLERIVAVAHAQDVPVLVDEAHGvHLPFHDELPLSAMQAGAD 123
Cdd:cd00609   146 GAvlsEEELEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAY 193
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 1-138 6.51e-07

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).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 45.84  E-value: 6.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSV-MSALVLTGAHPVFIhPEYDETYGIAHGitasAVERALELHPDTKAVLVINPTYF-G 78
Cdd:cd01494    32 AALLALLGPGDEVIVDANGHGSRyWVAAELAGAKPVPV-PVDDAGYGGLDV----AILEELKAKPNVALIVITPNTTSgG 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1532591145  79 VAGDLERIVAVAHAQDVPVLVDEAHGVHLPFHDELPLSAMqaGADVAATSVHK-LGGSMTG 138
Cdd:cd01494   107 VLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEG--GADVVTFSLHKnLGGEGGG 165
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
82-134 1.61e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 45.90  E-value: 1.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1532591145  82 DLERIVAVAHAQDVPVLVDEAHGV-HLPFHdelplsaMQA-GADVAATSVHKLGG 134
Cdd:COG0520   172 PVKEIAALAHAHGALVLVDGAQSVpHLPVD-------VQAlGCDFYAFSGHKLYG 219
GcvP1 COG0403
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ...
 1-99 1.70e-05

Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440172 [Multi-domain]  Cd Length: 442  Bit Score: 42.71  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIM--GVVGPNEKIIVPRNVHKSVMsALVLTGAHPVFIhpEYdETYGIAHGITASAVERALeLHPDTKAVLVINPTYFG 78
Cdd:COG0403   144 AMLMarRVTKRSNKVLVSEDVHPQTR-AVLKTYAEPLGI--EV-VEVPDEDGVTDLEALKAL-LDDDVAGVLVQYPNFFG 218

                          90       100
                  ....*....|....*....|.
gi 1532591145  79 VAGDLERIVAVAHAQDVPVLV 99
Cdd:COG0403   219 VIEDLRAIAEAAHAAGALVIV 239
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 1-105 1.96e-05

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 42.73  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAhpvfihpeydETYGIAHGiTASAVERALELHPDTKAVLVINPTYFGVA 80
Cdd:COG0156   112 GVISALAGRGDLIFSDELNHASIIDGARLSGA----------KVVRFRHN-DMDDLERLLKKARAARRKLIVTDGVFSMD 180

                          90       100
                  ....*....|....*....|....*...
gi 1532591145  81 GD---LERIVAVAHAQDVPVLVDEAHGV 105
Cdd:COG0156   181 GDiapLPEIVELAEKYGALLYVDDAHGT 208
PRK15029 PRK15029
arginine decarboxylase; Provisional
 10-79 2.58e-05

arginine decarboxylase; Provisional


Pssm-ID: 184989 [Multi-domain]  Cd Length: 755  Bit Score: 42.52  E-value: 2.58e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1532591145  10 NEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDEtYGI-----AHGITASAVERALELHPDTKAVLVINPTYFGV 79
Cdd:PRK15029  245 NDVVVVDRNCHKSIEQGLILTGAKPVYMVPSRNR-YGIigpiyPQEMQPETLQKKISESPLTKDKAGQKPSYCVV 318
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
12-125 2.97e-05

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 42.05  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145  12 KIIVPRNVHKSVMSAL--VLTGAHPVFIHPEYDETYgiahgITASAVERALElhPDTKAVLVINPTYFGVAGDLERIVAV 89
Cdd:PRK00451  156 KVLVSGAVHPEYREVLktYLKGQGIEVVEVPYEDGV-----TDLEALEAAVD--DDTAAVVVQYPNFFGVIEDLEEIAEI 228

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1532591145  90 AHAQDVPVLVdeahGVhlpfhDELPLSAMQA----GADVA 125
Cdd:PRK00451  229 AHAGGALFIV----GV-----DPVSLGLLKPpgeyGADIV 259
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
9-105 1.07e-04

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 40.37  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   9 PNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYGIahgiTASAVERALelhpDTKAVLVI-----NPTyfGVA--- 80
Cdd:pfam00155  86 PGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHL----DFDALEAAL----KEKPKVVLhtsphNPT--GTVatl 155

                          90       100
                  ....*....|....*....|....*
gi 1532591145  81 GDLERIVAVAHAQDVPVLVDEAHGV 105
Cdd:pfam00155 156 EELEKLLDLAKEHNILLLVDEAYAG 180
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 55-138 2.29e-04

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 39.37  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145  55 AVERALElhPDTKAVLVIN-PTYFGVAGDLERIVAVAHAQDVPVLVDEAHGV-HLPfhdeLPLSAMqaGADVAATSVHK- 131
Cdd:cd06453   131 ALEKLLT--ERTKLVAVTHvSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAgHMP----VDVQDL--GCDFLAFSGHKm 202


                  ....*..
gi 1532591145 132 LGGSMTG 138
Cdd:cd06453   203 LGPTGIG 209
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 1-105 2.91e-04

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 39.37  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAhpvfihpeydETYGIAHGiTASAVERALELHPDTKAVLVINpTYFGVA 80
Cdd:PRK05958  114 AVLTALAGKGDLIVSDKLNHASLIDGARLSRA----------RVRRYPHN-DVDALEALLAKWRAGRALIVTE-SVFSMD 181

                          90       100
                  ....*....|....*....|....*...
gi 1532591145  81 GD---LERIVAVAHAQDVPVLVDEAHGV 105
Cdd:PRK05958  182 GDlapLAELVALARRHGAWLLVDEAHGT 209
SelA COG1921
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
57-134 3.64e-04

Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441524  Cd Length: 399  Bit Score: 38.95  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145  57 ERALelHPDTKAVLVINPTYFGVAG-----DLERIVAVAHAQDVPVLVDEAHGVHLPF------HDELPLSAMQAGADVA 125
Cdd:COG1921   148 EAAI--TENTAALLKVHTSNYRIVGfteevSLAELAELAHEHGLPVIVDLGSGSLVDLskyglpHEPTVQEYLAAGADLV 225

                          90
                  ....*....|
gi 1532591145 126 ATSVHK-LGG 134
Cdd:COG1921   226 TFSGDKlLGG 235
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 13-134 6.09e-04

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 38.34  E-value: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145  13 IIVPRNVHKSVMSALVLTGAHPVFIhpEYDETYGIAHGITASAVERALELHPDTKAVLVINP-TYFGVAGDLERIVAVAH 91
Cdd:cd06450    98 IVCSDQAHVSVEKAAAYLDVKVRLV--PVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAGtTDTGAIDPLEEIADLAE 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1532591145  92 AQDVPVLVDEAHG-VHLPFHDELPLSAMQAGADVAATSVHKLGG 134
Cdd:cd06450   176 KYDLWLHVDAAYGgFLLPFPEPRHLDFGIERVDSISVDPHKYGL 219
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 1-105 7.61e-04

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 37.93  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAhPVFIHPEYDetygiahgitASAVERALE--LHPDTKaVLVINPTYFG 78
Cdd:cd06454    76 GVLSTLAGKGDLIISDSLNHASIIDGIRLSGA-KKRIFKHND----------MEDLEKLLReaRRPYGK-KLIVTEGVYS 143

                          90       100       110
                  ....*....|....*....|....*....|
gi 1532591145  79 VAGD---LERIVAVAHAQDVPVLVDEAHGV 105
Cdd:cd06454   144 MDGDiapLPELVDLAKKYGAILFVDEAHSV 173
SepCysS cd06452
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ...
 1-136 8.00e-04

Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.


Pssm-ID: 99745  Cd Length: 361  Bit Score: 38.14  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   1 AMIMGVVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYGIAHGITASAVERALELHPDTKAVLVIN-PTY-FG 78
Cdd:cd06452    74 AVMHSLCEKGDWVVVDGLAHYTSYVAAERAGLNVREVPNTGHPEYHITPEGYAEVIEEVKDEFGKPPALALLThVDGnYG 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1532591145  79 VAGDLERIVAVAHAQDVPVLVDEAHGVHLpfhdeLPLSAMQAGADVAATSVHKlggSM 136
Cdd:cd06452   154 NLHDAKKIAKVCHEYGVPLLLNGAYTVGR-----MPVSGKELGADFIVGSGHK---SM 203
PRK09331 PRK09331
Sep-tRNA:Cys-tRNA synthetase; Provisional
 2-136 9.13e-04

Sep-tRNA:Cys-tRNA synthetase; Provisional


Pssm-ID: 236469  Cd Length: 387  Bit Score: 37.99  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145   2 MIMG-VVGPNEKIIVPRNVHKSVMSALVLTGAHPVFIHPEYDETYGIAHGITASAVERALELHPDTKAVLVInpTY---- 76
Cdd:PRK09331   93 AVMHsLCKKGDYVVLDGLAHYTSYVAAERAGLNVREVPKTGYPEYKITPEAYAEKIEEVKEETGKPPALALL--THvdgn 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145  77 FGVAGDLERIVAVAHAQDVPVLVDEAHGVhlpfhDELPLSAMQAGADVAATSVHKlggSM 136
Cdd:PRK09331  171 YGNLADAKKVAKVAHEYGIPFLLNGAYTV-----GRMPVDGKKLGADFIVGSGHK---SM 222
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 22-100 2.55e-03

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 36.41  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145  22 SVMSALVLTGAHPVFIHPEYDETYGIAH------GITASAVERALE------LHPDTKAVLVINPT--YFGVAgDLERIV 87
Cdd:cd00614    70 TVLLALLKAGDHVVASDDLYGGTYRLFErllpklGIEVTFVDPDDPealeaaIKPETKLVYVESPTnpTLKVV-DIEAIA 148

                          90
                  ....*....|...
gi 1532591145  88 AVAHAQDVPVLVD 100
Cdd:cd00614   149 ELAHEHGALLVVD 161
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 12-138 3.22e-03

Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.


Pssm-ID: 99737 [Multi-domain]  Cd Length: 398  Bit Score: 36.44  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145  12 KIIVPRNVH---KSVMSalvlTGAHPvfihPEYD-ETYGIAHGITASAVERALELHPDTKAVLVINPTYFGVAGDLER-I 86
Cdd:cd00613   110 KVLVPDSAHptnPAVAR----TRGEP----LGIEvVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNTLGVFEDLIKeI 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1532591145  87 VAVAHAQDVPVLVDEAhgvhlpfhdelPLSAM------QAGADVAATSVHKLGGSMTG 138
Cdd:cd00613   182 ADIAHSAGALVYVDGD-----------NLNLTglkppgEYGADIVVGNLQKTGVPHGG 228
avtA PRK09440
valine--pyruvate transaminase; Provisional
 59-109 3.51e-03

valine--pyruvate transaminase; Provisional


Pssm-ID: 236517  Cd Length: 416  Bit Score: 35.99  E-value: 3.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1532591145  59 ALELHPDTKAVLV---INPTyfG-VAGD--LERIVAVAHAQDVPVLVDEAHGVhlPF 109
Cdd:PRK09440  173 HLHIDEDTGAICVsrpTNPT--GnVLTDeeLEKLDALARQHNIPLLIDNAYGP--PF 225
PRK10874 PRK10874
cysteine desulfurase CsdA;
82-138 4.32e-03

cysteine desulfurase CsdA;


Pssm-ID: 182799 [Multi-domain]  Cd Length: 401  Bit Score: 35.78  E-value: 4.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1532591145  82 DLERIVAVAHAQDVPVLVDEAHG-VHlpfhdeLPLSAMQAGADVAATSVHKLGGSmTG 138
Cdd:PRK10874  178 DLARAITLAHQAGMVVMVDGAQGaVH------FPADVQALDIDFYAFSGHKLYGP-TG 228
PRK07324 PRK07324
transaminase; Validated
 23-112 5.52e-03

transaminase; Validated


Pssm-ID: 235989  Cd Length: 373  Bit Score: 35.68  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532591145  23 VMSALVLTGAHPVFIHPEYDETYGIAHGITASAveRALELH-----------------PDTKAVLVINP-----TYFGVA 80
Cdd:PRK07324   96 VLYALVEPGDHVISVYPTYQQLYDIPESLGAEV--DYWQLKeengwlpdldelrrlvrPNTKLICINNAnnptgALMDRA 173

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1532591145  81 GdLERIVAVAHAQDVPVLVDEahgVHLPFHDE 112
Cdd:PRK07324  174 Y-LEEIVEIARSVDAYVLSDE---VYRPLDED 201
 
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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