ID A0A1U9K4V1_9BACL Unreviewed; 451 AA.
AC A0A1U9K4V1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=4-aminobutyrate--2-oxoglutarate transaminase {ECO:0000313|EMBL:AQS55075.1};
GN ORFNames=B0W44_04085 {ECO:0000313|EMBL:AQS55075.1};
OS Novibacillus thermophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Novibacillus.
OX NCBI_TaxID=1471761 {ECO:0000313|EMBL:AQS55075.1, ECO:0000313|Proteomes:UP000188603};
RN [1] {ECO:0000313|EMBL:AQS55075.1, ECO:0000313|Proteomes:UP000188603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-1 {ECO:0000313|EMBL:AQS55075.1,
RC ECO:0000313|Proteomes:UP000188603};
RX PubMed=25951858; DOI=10.1099/ijs.0.000306;
RA Yang G., Chen J., Zhou S.;
RT "Novibacillus thermophilus gen. nov., sp. nov., a Gram-staining-negative
RT and moderately thermophilic member of the family Thermoactinomycetaceae.";
RL Int. J. Syst. Evol. Microbiol. 65:2591-2597(2015).
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; CP019699; AQS55075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9K4V1; -.
DR STRING; 1471761.B0W44_04085; -.
DR KEGG; ntr:B0W44_04085; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000188603; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000188603}.
SQ SEQUENCE 451 AA; 50260 MW; 216289969A296A48 CRC64;
MGERKFANVQ TELPGPKAKE WLKRRLNIVP DAVSYGVPTF VQSAKGAILH DVDGNTFIDF
AGAIGTINIG HCHDSVVEAL HDQIDRYIHT GFNVMMYDPY IQLAEKMAAI SPGNCEKKVM
FFNSGAEAVE NAVKIARKFT KRNAVVSFTG GFHGRTLMAM SLTGKVKPYK HEFGPFAPEI
YRAPFPYAYR RPENMNEEEY IRFVLDQLDD FFLREVDPNL VAAVIMEPVQ GEGGFIIPGK
QFVQEVYERC KKYGILFIAD EIQTGFGRTG RYFAVEHYGI EPDLITISKS MAAGLPISGV
IGRREVMDQA GSGELGGTYC GSPLGCRAGL AVLEAMEQEK MNERATEIGE KVMRKFKAMY
DRFDVIGDVR GLGAMCALEL VKDRKSKEPH KELCNRILQE AYTRGLIVLK AGVFDNVIRL
LMPLVITDDE LEEGLSILEE SIETALALQL N
//
