ID   I6UZZ1_9EURY            Unreviewed;       459 AA.
AC   I6UZZ1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AFN03308.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:AFN03308.1};
GN   ORFNames=PFC_01685 {ECO:0000313|EMBL:AFN03308.1};
OS   Pyrococcus furiosus COM1.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=1185654 {ECO:0000313|Proteomes:UP000006216};
RN   [1] {ECO:0000313|EMBL:AFN03308.1, ECO:0000313|Proteomes:UP000006216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COM1 {ECO:0000313|EMBL:AFN03308.1,
RC   ECO:0000313|Proteomes:UP000006216};
RX   PubMed=22636780; DOI=10.1128/JB.00439-12;
RA   Bridger S.L., Lancaster W.A., Poole F.L.II., Schut G.J., Adams M.W.;
RT   "Genome Sequencing of a Genetically-Tractable Pyrococcus furiosus Strain
RT   Reveals a Highly Dynamic Genome.";
RL   J. Bacteriol. 194:4097-4106(2012).
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|RuleBase:RU003560}.
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DR   EMBL; CP003685; AFN03308.1; -; Genomic_DNA.
DR   RefSeq; WP_011011630.1; NC_018092.1.
DR   AlphaFoldDB; I6UZZ1; -.
DR   GeneID; 41712315; -.
DR   KEGG; pfi:PFC_01685; -.
DR   PATRIC; fig|1185654.4.peg.343; -.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   Proteomes; UP000006216; Chromosome.
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   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; 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   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:AFN03308.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AFN03308.1}.
SQ   SEQUENCE   459 AA;  50555 MW;  4B7BD1DAE13D7DA0 CRC64;
     MEYPKIITKL PGPKATEIIE RESRILSPGI GVKLFPLVPK RGFGALIEDV DGNIFIDFLA
     GAAAASTGYS HPKLVKAVQE QVALIQHSMI GYTHNERAIR VAEKLAKISP IKNPRIIFGM
     SGSDAVDMAI KVSKFSTRRP WILSFIGAYH GQTLGATSIA AFQSSQKRGF SPLMPNVIWL
     PYPNPYRNIW GIDGYEEPNE LINRFLDYLE NYVFSHLSPS DEVAALFAEP IQGDAGIVVP
     PENFFKEVQK VLNDLGILLV MDEVQTGIGR TGKWFASEWF SVEPDLIIFG KGVASGMGLS
     GVIGRKELMD LTSGAALLTP AANPVVSAAA EATLEIIEEE NLLENALKVG NFIKKRLEEM
     KEVFEVIGDV RGKGLMIGVE IVKDRESKKP DPELTGKICW RAFELGLILP SYGMFQNVIR
     ITPPLVITQE IAEKGLEIME RAIKDALAGK VERKVVTWH
//