ID   Q8ERP0_OCEIH            Unreviewed;       434 AA.
AC   Q8ERP0;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAC13217.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:BAC13217.1};
GN   OrderedLocusNames=OB1261 {ECO:0000313|EMBL:BAC13217.1};
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 /
OS   KCTC 3954 / HTE831).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109 {ECO:0000313|EMBL:BAC13217.1, ECO:0000313|Proteomes:UP000000822};
RN   [1] {ECO:0000313|EMBL:BAC13217.1, ECO:0000313|Proteomes:UP000000822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831
RC   {ECO:0000313|Proteomes:UP000000822};
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13217.1; -; Genomic_DNA.
DR   RefSeq; WP_011065663.1; NC_004193.1.
DR   AlphaFoldDB; Q8ERP0; -.
DR   STRING; 221109.gene:10733501; -.
DR   KEGG; oih:OB1261; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_9; -.
DR   OrthoDB; 9807885at2; -.
DR   PhylomeDB; Q8ERP0; -.
DR   Proteomes; UP000000822; 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:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 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:BAC13217.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000822};
KW   Transferase {ECO:0000313|EMBL:BAC13217.1}.
SQ   SEQUENCE   434 AA;  47734 MW;  4A024EE26D93CCED CRC64;
     MNKSDQHWQE LVNSIGNFLA PSMAKDHPNL PVVKAEGCYY YGTDGKEYLD FTSGIAVENV
     GHRHPKVVQA IKDSADHLVH GPSGVIIYES ILKLAQELQE IMPPKLDNFF FANSGTEAIE
     GGLKLAKHVT KRPYVISFTG NFHGRSIGSL SVSTSKSKYR KYQQPSWLTY QLPYALPEYL
     PEGQDPEVFF AEKLEKDAES LFKHQVDPEE VACMILEPIM GEGGYIIPPK SWLQKVREIC
     DRHGILLIFD EVQTGFGRTG DWFAAQTFGV TPDIMAIAKG IAAGMPLSAT VASKELMDQW
     PLGSHGTTFG GNPIACAAAR ASLSIMKEEK LLNNAKTMGD YALTKLSGLK DKYEIVHEVR
     GIGLMLGIEL RDPETGEPDG EAVMKALNGC LDEGVLFYLC GNAGEVIRMI PPLTINKEQI
     DQGIDVLDKV LAQM
//