ID A0A109QHC2_9BACL Unreviewed; 442 AA.
AC A0A109QHC2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AMA73654.1};
GN ORFNames=ACH33_12835 {ECO:0000313|EMBL:AMA73654.1};
OS Aneurinibacillus sp. XH2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA73654.1, ECO:0000313|Proteomes:UP000065566};
RN [1] {ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA Xi L.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMA73654.1, ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|EMBL:AMA73654.1,
RC ECO:0000313|Proteomes:UP000065566};
RA Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT China.";
RL Submitted (JAN-2016) 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; CP014140; AMA73654.1; -; Genomic_DNA.
DR RefSeq; WP_057899382.1; NZ_CP014140.1.
DR AlphaFoldDB; A0A109QHC2; -.
DR STRING; 1450761.ACH33_12835; -.
DR KEGG; anx:ACH33_12835; -.
DR Proteomes; UP000065566; 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; 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; ORNITHINE AMINOTRANSFERASE; 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:AMA73654.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000065566};
KW Transferase {ECO:0000313|EMBL:AMA73654.1}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 47916 MW; E4E959772F69758B CRC64;
MTTNAQTSQG PKSAKLHARR QEAVPVGPYH VTPLYIQSAQ GAIVTDVDGN ELIDFAGGIG
MQNIGHCHPK VVKAIQEQAA ASIHSCFHVM PYESYIELAE KLNEKTPGDF KKKTMFANSG
AEAVENAVKI ARKATGRSAV VSFERGYHGR TLMTMSLTSK VNPYKHGFGP FAPETYKLPY
PYYYRAPQGM LPEELDEQVL HHFEQFFLGE VGADHIAAII MEPVQGEGGF IVPSTTFVQG
VRRICDKYGI LMIADEIQTG FARTGKLFAM ENYGVAADIT TMSKSIAAGM PLSAITGRAE
LMDAPGAGQL GGTFAGSPVA CAAGLAVLDV IEEENLVERA QVIGDRMMNA FRSWQEKYDL
IGDVRGLGAM VALELVRDRV TKEPAKEETG KIVTECWNNG LIGLSAGIFG NVLRFLPPLV
ITDEHLEKGL HILEQAIAKA SK
//