UniProt: D4MTR2

Database: UniProt
Entry: D4MTR2_ANAHA

LinkDB:  D4MTR2_ANAHA 
Original site:  D4MTR2_ANAHA

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Ontology (2)   
   GO (2)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (8)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (1)   
All databases (16)   

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ID   D4MTR2_ANAHA            Unreviewed;       377 AA.
AC   D4MTR2;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Serine-pyruvate aminotransferase/archaeal aspartate aminotransferase {ECO:0000313|EMBL:CBL38778.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:CBL38778.1};
DE   SubName: Full=Soluble hydrogenase 42 kDa subunit {ECO:0000313|EMBL:CUM91105.1};
DE            EC=1.12.-.- {ECO:0000313|EMBL:CUM91105.1};
GN   ORFNames=CL2_18790 {ECO:0000313|EMBL:CBL38778.1}, ERS852425_01414
GN   {ECO:0000313|EMBL:CUM91105.1}, ERS852520_00027
GN   {ECO:0000313|EMBL:CUO86715.1};
OS   Anaerostipes hadrus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL38778.1, ECO:0000313|Proteomes:UP000008960};
RN   [1] {ECO:0000313|EMBL:CBL38778.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38778.1,
RC   ECO:0000313|Proteomes:UP000008960};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SSC/2.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL38778.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38778.1,
RC   ECO:0000313|Proteomes:UP000008960};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000095564, ECO:0000313|Proteomes:UP000095598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5608868 {ECO:0000313|EMBL:CUM91105.1,
RC   ECO:0000313|Proteomes:UP000095598}, and 2789STDY5834908
RC   {ECO:0000313|EMBL:CUO86715.1, ECO:0000313|Proteomes:UP000095564};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC       ECO:0000256|RuleBase:RU004075}.
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DR   EMBL; FP929061; CBL38778.1; -; Genomic_DNA.
DR   EMBL; CYXT01000008; CUM91105.1; -; Genomic_DNA.
DR   EMBL; CZAU01000001; CUO86715.1; -; Genomic_DNA.
DR   RefSeq; WP_008392220.1; NZ_WQRA01000007.1.
DR   AlphaFoldDB; D4MTR2; -.
DR   STRING; 649756.ERS852387_01717; -.
DR   GeneID; 15231869; -.
DR   KEGG; bprl:CL2_18790; -.
DR   PATRIC; fig|245018.3.peg.2163; -.
DR   OrthoDB; 389074at2; -.
DR   Proteomes; UP000008960; Chromosome.
DR   Proteomes; UP000095564; Unassembled WGS sequence.
DR   Proteomes; UP000095598; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CBL38778.1};
KW   Oxidoreductase {ECO:0000313|EMBL:CUM91105.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:CBL38778.1};
KW   Transferase {ECO:0000313|EMBL:CBL38778.1}.
FT   DOMAIN          30..321
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         191
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   377 AA;  41550 MW;  EB859265C1CC89D2 CRC64;
     MSKYKIMTPG PVQVPENVRL ARSLSTTNAD LDPQFYDEYK ETCELISELL HTKNETLILS
     GEGILGLEAA CASMTEPGDR VLILDNGIYG AGFADFVSMY GGTPVMYTKD YKNAFDVDEL
     DAYLKEDHDF KYATVVHCDT PSGMLNDIHK ICPLLKSYGI MTVTDSVSGM FGNEVNVDKA
     QIDILCGGSQ KAVSAPPGLT FVTISDEAKK AMENRKTPIA SFYCNLTIFK DYYKNLWFPY
     TMPISDIYGL KAAMDNIAAD KDLIKRHARI ANATRKAIEA FGLKLHLESG FSDTVTVFDV
     PEGMTADDIL ERMREKHGIM LAGSFGELAG KVIRIGHMGA SANVGDMLEV MSGLEETLRY
     LGWKSENSLL GVFHTEL
//

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