ID G4F994_9GAMM Unreviewed; 425 AA.
AC G4F994;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:EHA14756.1};
GN ORFNames=HAL1_14871 {ECO:0000313|EMBL:EHA14756.1};
OS Halomonas sp. HAL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA14756.1, ECO:0000313|Proteomes:UP000005692};
RN [1] {ECO:0000313|EMBL:EHA14756.1, ECO:0000313|Proteomes:UP000005692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX PubMed=22156396; DOI=10.1128/JB.06359-11;
RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA Wang G., Rensing C.;
RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL J. Bacteriol. 194:199-200(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:EHA14756.1}.
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DR EMBL; AGIB01000071; EHA14756.1; -; Genomic_DNA.
DR RefSeq; WP_008958847.1; NZ_CP130610.1.
DR AlphaFoldDB; G4F994; -.
DR PATRIC; fig|550984.5.peg.2868; -.
DR Proteomes; UP000005692; 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 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:EHA14756.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EHA14756.1}.
SQ SEQUENCE 425 AA; 45542 MW; D6E4785E72A50891 CRC64;
MSSNAELNEL KHKYVAAGAA SPATAFADRA ENSEIWDVDG NRFIDFAGGI GVLNVGHRHP
KVVAAVKAQL DKLMHTCQTV MPYEGYVKVA EKLSQIVPVR GHAKVMLANS GAEALENAVK
IARAATGRSN VICFDGGYHG RTFFTMAMNG KVAPYQSDFG PMPGTVFRAP YPVPYHGVSE
DEAIRGLKMT LKTDANPKDT AAIVLEPVLG EGGFYPASTS FLTKIREICD EHGILMIIDE
VQSGFGRTGK MFAIEHSGVE PDIMTMAKSM ADGMPISAIV GTDKVMDASG PNSLGGTYTG
SPTACAAALA VMEVFEEENI LEKSQALGDK LAKRFNEWAG KFDCIDNVRN MGSMAAFELV
SNKADHTPNA ELAAALCKKA REEGLILLSC GMYGNTIRFL MPVTIQDDVL NEGLDIIESC
LESLT
//
