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Database: UniProt
Entry: A0A2S4XKC5_9ACTN
LinkDB: A0A2S4XKC5_9ACTN
Original site: A0A2S4XKC5_9ACTN 
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}.
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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
//
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