ID A0A2S4XKC5_9ACTN Unreviewed; 449 AA.
AC A0A2S4XKC5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=4-aminobutyrate--2-oxoglutarate transaminase {ECO:0000313|EMBL:POX37019.1};
GN Name=gabT {ECO:0000313|EMBL:POX37019.1};
GN ORFNames=C3486_30515 {ECO:0000313|EMBL:POX37019.1};
OS Streptomyces sp. Ru73.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080748 {ECO:0000313|EMBL:POX37019.1, ECO:0000313|Proteomes:UP000236956};
RN [1] {ECO:0000313|EMBL:POX37019.1, ECO:0000313|Proteomes:UP000236956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru73 {ECO:0000313|EMBL:POX37019.1,
RC ECO:0000313|Proteomes:UP000236956};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-2018) 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 -!- 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:POX37019.1}.
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; PQSQ01000101; POX37019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4XKC5; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000236956; 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:0009058; P:biosynthetic process; IEA:UniProt.
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:UP000236956}.
SQ SEQUENCE 449 AA; 47165 MW; 9F64D057FA819225 CRC64;
MSELTGGPAL PQERRVVTAI PGPKSQELWA RKQETVAAGV GAVLPVFIKR AGGGVLEDVD
GNSLIDFGSG IAVTSVGSSA EAVVRRAAAQ LADFTHTCAM VTPYEPYLEV CEALAELTPG
DHAKKSALFN SGAEAVENAV KIARAYTKRQ AVVVFDHGYH GRTNLTMALT AKNMPYKHGF
GPFAPEVYRV PLAYPYRWLT GPENCAQEAA DQAISQITKQ IGAENVAAII IEPVLGEGGF
IEPAKGFLPA MAKFAKDNGI VFVADEIQSG FCRTGQWFAC EDEGIVPDLI TTAKGIAGGL
PLAAVTGRAE IMDAAHAGGL GGTYGGNPVA CAAAVGAIET MRELDLNAKA QRIEEVMKSR
LATMAEKYDI IGEVRGRGAM IAIELVQSGS KDPNPEATSA LAKACHQEGL LILTTGTYGN
VIRFLPPLVI GEDLLNEGLD ILESAFAAL
//