ID A0A074JUD8_9RHOB Unreviewed; 421 AA.
AC A0A074JUD8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KEO61291.1};
GN ORFNames=DT23_09365 {ECO:0000313|EMBL:KEO61291.1};
OS Thioclava indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO61291.1, ECO:0000313|Proteomes:UP000027471};
RN [1] {ECO:0000313|EMBL:KEO61291.1, ECO:0000313|Proteomes:UP000027471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DT23-4 {ECO:0000313|EMBL:KEO61291.1,
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 -!- 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:KEO61291.1}.
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DR EMBL; AUNB01000002; KEO61291.1; -; Genomic_DNA.
DR RefSeq; WP_038127870.1; NZ_AUNB01000002.1.
DR AlphaFoldDB; A0A074JUD8; -.
DR STRING; 1353528.DT23_09365; -.
DR eggNOG; COG0160; Bacteria.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000027471; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 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:KEO61291.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000027471};
KW Transferase {ECO:0000313|EMBL:KEO61291.1}.
SQ SEQUENCE 421 AA; 45372 MW; 967AA85727F01CA4 CRC64;
MENELMARRA RLLGPNVPTF YEQPVHITRG AGAYLWDAQD QRYLDAYNNV AHVGHCHPRV
VRAIADQAAT LNTHTRYLHE GILDYGEALV ARLDHGLNQL LMTCTGSEAN DVALRMAQAV
TGKRGFIATD NTYHGNTTAV AHLSTRRPPI GGWPDHIRRV PAPDSLAPLG GSLDAQPRAF
AANVAQAIAE LETSGHGFAG FMLCPIFANE GMPGVTPGFL NPTVEIIRQA GGLIIADEVQ
PGFGRIGSHF WGHDWLGFAP DVVTLGKPMG NGHPVAGVVA RADVMAAFRE AFGYFNTFGG
NPVSCAAAMA VLQVIDDEEL QQNAAEIGAY LLQGLRSIEH PLIADTRGLG LFAAIELARD
GQPASAEAGQ IVEAMRNRHV LMGRVGRAQH ILKIRPPLVF SRQEVDFLID QLRASFAEIP
A
//
