ID A0A0M1JA71_9GAMM Unreviewed; 405 AA.
AC A0A0M1JA71;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Succinyldiaminopimelate aminotransferase {ECO:0000313|EMBL:KOR30176.1};
GN ORFNames=TI03_00170 {ECO:0000313|EMBL:KOR30176.1};
OS Achromatium sp. WMS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604834 {ECO:0000313|EMBL:KOR30176.1, ECO:0000313|Proteomes:UP000036736};
RN [1] {ECO:0000313|EMBL:KOR30176.1, ECO:0000313|Proteomes:UP000036736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS1 {ECO:0000313|EMBL:KOR30176.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KOR30176.1}.
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; JXSM01000004; KOR30176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1JA71; -.
DR PATRIC; fig|1604834.3.peg.679; -.
DR Proteomes; UP000036736; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009016; F:succinyldiaminopimelate transaminase activity; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR019878; DapC_beta/gammaproteobac.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03538; DapC_gpp; 1.
DR PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:KOR30176.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036736};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOR30176.1}.
FT DOMAIN 33..396
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 405 AA; 45271 MW; B13C87D3F7D57C61 CRC64;
MNANIAKLQS YPFARLNQLK AQVQPSNNLA PIRLEIGEPQ EQTPKFINDT IITNLQSLQA
YPNTKGLPEL RQAIAKWLSW RFALPEKSLD SETQILPVNG TREALFAFAQ VIINTSNNAQ
NTTAQPLVMM PNPFYQIYEG AALLAGAEPY FIPYIDKLAP DFAAVSPKDW QRCQLLYICS
PGNPTGSVLD LATLQYIIKL ADQYDFVIAA DECYSEIYQD ESTPPPGLLQ AAATLGRTDY
RRCVVFNSLS KRSNCPGLRS GFVAGDATIL QHFFLYRTYH GCAMSIYAQK ASTAAWSDER
HVHTNRDLYR EKFAAVTTIL NPVLPVTIPA ATFYLWIETA ISDTEFAQNL FAYKNVTVLP
GSFLARNVTG QPNPGHKRVR IALTPKLEVC IEAAQRIRHY IEIIS
//