ID A0A074JV79_9RHOB Unreviewed; 424 AA.
AC A0A074JV79;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KEO60389.1};
GN ORFNames=DT23_02575 {ECO:0000313|EMBL:KEO60389.1};
OS Thioclava indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO60389.1, ECO:0000313|Proteomes:UP000027471};
RN [1] {ECO:0000313|EMBL:KEO60389.1, ECO:0000313|Proteomes:UP000027471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DT23-4 {ECO:0000313|EMBL:KEO60389.1,
RC ECO:0000313|Proteomes:UP000027471};
RX PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT Ocean.";
RL Antonie Van Leeuwenhoek 107:297-304(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}.
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:KEO60389.1}.
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DR EMBL; AUNB01000018; KEO60389.1; -; Genomic_DNA.
DR RefSeq; WP_038129524.1; NZ_AUNB01000018.1.
DR AlphaFoldDB; A0A074JV79; -.
DR STRING; 1353528.DT23_02575; -.
DR eggNOG; COG0160; Bacteria.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000027471; 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; 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 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:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:KEO60389.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000027471};
KW Transferase {ECO:0000313|EMBL:KEO60389.1}.
SQ SEQUENCE 424 AA; 44849 MW; EDDD5BDD2087E90D CRC64;
MSSNIELETR RAAALARGVG VQTKNFAVSA ENATVTDADG NTLIDFAAGI AVVNTGHRHP
KVIEAVKAQL DAFTHTCHQV LPYEPYVRLA ERLNDKVPGD FDKKSIFVTT GAESVENAVK
IARAYTGRNA VIAFGGGFHG RTFMTMSLTG KVAPYKAGFG SMMPDVFHIP FPNALHGVSV
EDSFAAMESL FKTDLDPARL AAVIFEPVQG EGGFVPAPRD FVLRLREFCD QHGIVMIADE
VQSGFARTGT LFAMEAFGVA ADITTMAKGL GGGLPIAAVT GRADIMDAAN PGGLGGTYGG
NPLGVAAGNA VLDVIEEEDL CSRANELGSR LKQRLEQIRD KMPEIAEIRG PGFMVAIELM
QDGKPAPDLT KAVQAEALSR GLLLLSCGVY GNVIRFLAPI TIPDAQMSQA LDILEEAMLA
AKGA
//
