ID H0J5N2_9GAMM Unreviewed; 423 AA.
AC H0J5N2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:EHK59758.1};
GN ORFNames=MOY_14752 {ECO:0000313|EMBL:EHK59758.1};
OS Halomonas sp. GFAJ-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK59758.1, ECO:0000313|Proteomes:UP000004512};
RN [1] {ECO:0000313|EMBL:EHK59758.1, ECO:0000313|Proteomes:UP000004512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK59758.1,
RC ECO:0000313|Proteomes:UP000004512};
RX PubMed=22408239; DOI=10.1128/JB.06664-11;
RA Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL J. Bacteriol. 194:1835-1836(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|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:EHK59758.1}.
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DR EMBL; AHBC01000052; EHK59758.1; -; Genomic_DNA.
DR RefSeq; WP_009101244.1; NZ_CP016490.1.
DR AlphaFoldDB; H0J5N2; -.
DR STRING; 1118153.MOY_14752; -.
DR KEGG; hag:BB497_05750; -.
DR PATRIC; fig|1118153.6.peg.3001; -.
DR eggNOG; COG0160; Bacteria.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000004512; Unassembled WGS sequence.
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 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:EHK59758.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000004512};
KW Transferase {ECO:0000313|EMBL:EHK59758.1}.
SQ SEQUENCE 423 AA; 45013 MW; 0673C30D5EA5C587 CRC64;
MTNQELNDLK NRFVANGAAT PTTQFAERAE NAELWDADGK RWIDFAGGIG VLNLGHRHPK
IVAAVEAQLK KVMHTSAAVI SYAPYVQLCQ KLCELTPVRG PERKAMLVNT GAEALENAVK
IARAATGRTG IITFDGAFHG RTMMTLAMTG KVLPYKNDFG PMPGDVFRAP FPNPLHGISE
EASLSAIRTL FKTDIAPHRT AAIVIEPVQG EGGFYIASPD YLKALRALCD EHGILLIADE
VQSGFARTGK LFALEHSGIE ADILTTAKSL ANGMPLSAVV GTAKVMDASG PNSLGGTYSG
NPLSCAAALA VIEAIEEENI LARSEQMGNM LAERFAVWGE RFPAVAHGRQ LGAMAAFELL
NVEGKPDPQM TGALCAKARE KGLILLSCGF YGNSIRILVP LTVSSAVLEE GLSIIEESLE
ALS
//
