ID   Q0HSC7_SHESR            Unreviewed;       425 AA.
AC   Q0HSC7;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABI43978.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABI43978.1};
GN   OrderedLocusNames=Shewmr7_2994 {ECO:0000313|EMBL:ABI43978.1};
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481 {ECO:0000313|EMBL:ABI43978.1};
RN   [1] {ECO:0000313|EMBL:ABI43978.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MR-7 {ECO:0000313|EMBL:ABI43978.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of Chromosome1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000444; ABI43978.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0HSC7; -.
DR   KEGG; shm:Shewmr7_2994; -.
DR   HOGENOM; CLU_016922_10_0_6; -.
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:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ABI43978.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABI43978.1}.
SQ   SEQUENCE   425 AA;  44713 MW;  58154059F9FFE92D CRC64;
     MSTTNDSLMA RRQAAVAGGV GQIHPVFTAR AENATVWDVE GREFIDFAGG IAVLNTGHLH
     PKVKAAVAAQ LEDFSHTCFM VLGYESYIQV CEKLNQLVPG DFAKKTALFT SGSEAVENAV
     KVARAYTKRA GVIAFTSGYH GRTMAALALT GKVAPYSKGM GLMSANVFRA EFPCALHGVS
     DDDAMASIER IFKNDAEPSD IAAIILEPVQ GEGGFYAASP AFMQRLRALC DREGIMLIAD
     EVQTGAGRTG TFFAMEQMGV SADITTFAKS IAGGFPLSGI TGKAEVMDAI GPGGLGGTYG
     GNPLACAAAL AVLEVFEEEK LLERANAIGE RIKSALNTMQ VEHPQIADVR GLGAMIAIEL
     MEDGKPAPQY CAQILAEARN RGLILLSCGT YGNVLRILVP LTVPDEQLGA GLGILKACFD
     AVLKG
//