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Database: UniProt
Entry: A0A495XIT9_9PSEU
LinkDB: A0A495XIT9_9PSEU
Original site: A0A495XIT9_9PSEU 
ID   A0A495XIT9_9PSEU        Unreviewed;       428 AA.
AC   A0A495XIT9;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   13-SEP-2023, entry version 12.
DE   SubName: Full=4-aminobutyrate aminotransferase/(S)-3-amino-2-methylpropionate transaminase {ECO:0000313|EMBL:RKT73987.1};
GN   ORFNames=DFJ66_7329 {ECO:0000313|EMBL:RKT73987.1};
OS   Saccharothrix variisporea.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT73987.1, ECO:0000313|Proteomes:UP000272729};
RN   [1] {ECO:0000313|EMBL:RKT73987.1, ECO:0000313|Proteomes:UP000272729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT73987.1,
RC   ECO:0000313|Proteomes:UP000272729};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-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:RKT73987.1}.
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DR   EMBL; RBXR01000001; RKT73987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495XIT9; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000272729; 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; 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   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:RKT73987.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272729};
KW   Transferase {ECO:0000313|EMBL:RKT73987.1}.
SQ   SEQUENCE   428 AA;  44601 MW;  5A09ED555FD22F82 CRC64;
     MTRLLTQIPG PRSQELTARR KGAVSAAVGS TLPVFVDHAE DGLLVDVDGN RLIDLGSGIA
     VTGVGNPAPR VAEAVHRQID RFSHTCFMVT PYEGYVEVCE RLNELTPGTH EKRSALFNSG
     AEAVENAVKV ARHATGRQAV VVFDHGYHGR TNLTMALTAK NMPYKHGFGP FAPEVYRVPA
     SYPFRDGLGG EEAAARAVEA IEKQVGADNT ACVVIEPIQG EGGFIVPAPG FLPALARWCR
     DRGVVLVADE IQTGFCRTGS WFASDHEGVV PDLVTTAKGI AGGLPLAGVT GRAELVDAVH
     VGGLGGTYGG NPVACAAALG AIDTMVERDL NAAARRIEEY VVPRLRAALG DGGEVRGRGA
     MLAVEFAERT PAVAARVAAA CHAAGVVVLT CGTYGNVLRL LPPLVIPDDL LAEGVAVVER
     AINGGVAG
//
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