ID W6N232_CLOTY Unreviewed; 459 AA.
AC W6N232;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase {ECO:0000313|EMBL:CDL90383.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:CDL90383.1};
GN ORFNames=CTDIVETGP_0453 {ECO:0000313|EMBL:CDL90383.1};
OS Clostridium tyrobutyricum DIVETGP.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1408889 {ECO:0000313|EMBL:CDL90383.1, ECO:0000313|Proteomes:UP000019482};
RN [1] {ECO:0000313|EMBL:CDL90383.1, ECO:0000313|Proteomes:UP000019482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DIVETGP {ECO:0000313|EMBL:CDL90383.1,
RC ECO:0000313|Proteomes:UP000019482};
RA Soggiu A., Piras C., Gaiarsa S., Sassera D., Roncada P., Bendixen E.,
RA Brasca M., Bonizzi L.;
RT "Draft Genome Sequence of Clostridium tyrobutyricum Strain DIVETGP,
RT Isolated from Cow's Milk for Grana Padano Production.";
RL Genome Announc. 3:213-215(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL90383.1}.
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DR EMBL; CBXI010000006; CDL90383.1; -; Genomic_DNA.
DR RefSeq; WP_017753040.1; NZ_CBXI010000006.1.
DR AlphaFoldDB; W6N232; -.
DR GeneID; 29419419; -.
DR Proteomes; UP000019482; Unassembled WGS sequence.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
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; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CDL90383.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000019482};
KW Transferase {ECO:0000313|EMBL:CDL90383.1}.
SQ SEQUENCE 459 AA; 50095 MW; 3F7F647DB031B01E CRC64;
MIKENSAKIV TEIPGPKSKE LISKRQKYVA KGVGCSAPIF VDEAKGALIK DIDGNVFVDF
AGAIGVQNIG HRDDGVVEAV KAQLDKYIHP SFHVNMYEPY INLAEKLVEV TPGDYAKKAM
FANSGAEAVE NAIKIARAYT KKAGVISLQG SFHGRTNMTM SITSKYKPYK NGFGPFSTET
YKTDAAYCYR CPLGCKYPEC GIACAEKLRT MLKTVISSDM IACLIAEPVQ GEGGFVVPPK
EYFKILQEIC NENGIVFIID EVQAGFARTG KLFAHEHFDV EADIVTMSKS IANGIPLSAV
VGKAEIMDAA CVGGIGGTYG GSPLGCVAAL KVIEKIKNDK LCDKSRKMGE YIIKRLNAMK
EKYDVIGDVR GLGSMIGLEF VKDRVTKEPY GELVKQITEY CFKHGVIFLN AGLFGNVVRF
LPPLVITKEQ LDYGLNVLDK AIDISLCKQN SPVKKKIVF
//