ID   A9L4Z5_SHEB9            Unreviewed;       425 AA.
AC   A9L4Z5;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABX48380.1};
GN   OrderedLocusNames=Sbal195_1205 {ECO:0000313|EMBL:ABX48380.1};
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX48380.1, ECO:0000313|Proteomes:UP000000770};
RN   [1] {ECO:0000313|EMBL:ABX48380.1, ECO:0000313|Proteomes:UP000000770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195 {ECO:0000313|EMBL:ABX48380.1,
RC   ECO:0000313|Proteomes:UP000000770};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000891; ABX48380.1; -; Genomic_DNA.
DR   RefSeq; WP_012196786.1; NC_009997.1.
DR   AlphaFoldDB; A9L4Z5; -.
DR   GeneID; 11771481; -.
DR   KEGG; sbn:Sbal195_1205; -.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   Proteomes; UP000000770; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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:ABX48380.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABX48380.1}.
SQ   SEQUENCE   425 AA;  44756 MW;  745CBA969500D17F CRC64;
     MTTTNDSLMA RRQAAVAGGV GQIHPIFTAR AENATVWDVE GREFIDFAGG IAVLNTGHLH
     PKVKAAVAAQ LDNFSHTCFM VLGYESYIQV CEKLNQLVPG DFAKKTALFT SGSEAVENAV
     KVARAYTKRA GVIAFTSGYH GRTIAALALT GKVAPYSKGM GLMSANVFRA EFPCEMHGVS
     DDDAMASIER IFKNDAEPSD IAAIILEPVQ GEGGFYAASP AFMQRLRALC DREGIMLIAD
     EVQTGAGRTG TFFAMEQMGV SADITTFAKS IAGGFPLSGI TGRAQVMDAI GPGGLGGTYG
     GSPLACAAAL AVIEVFEEEK LLDRANTIGE RIKSALNVMQ VEHAQIADVR GLGAMIAIEL
     MEDGKPAPHY CAQVLSDARD RGLILLSCGT YGNVLRILVP LTAPDAQIDA GLGILKASFD
     AVLKS
//