ID A0A101GSY8_9FIRM Unreviewed; 369 AA.
AC A0A101GSY8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:KUK63964.1};
GN ORFNames=XD84_1844 {ECO:0000313|EMBL:KUK63964.1};
OS Desulfotomaculum sp. 46_80.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1641375 {ECO:0000313|EMBL:KUK63964.1, ECO:0000313|Proteomes:UP000053828};
RN [1] {ECO:0000313|Proteomes:UP000053828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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:KUK63964.1}.
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DR EMBL; LGGF01000050; KUK63964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101GSY8; -.
DR PATRIC; fig|1641375.3.peg.322; -.
DR Proteomes; UP000053828; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 181
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 369 AA; 40570 MW; FF2280A6C7711422 CRC64;
MQVPLSLPDL SEREIEAVTA VLKSRWLSMG PAVEDFESKF AGYIGVKHAV AVNSGTSGLH
LAVRSLGIGK GDEAITTPFS FVSSANCLLF EGARPVFADI DPETLNIDCS LIENKINKNT
KCLLPVHIFG QPVDMSLIRS IASRHGLSVL EDSCEAIGAR YNSRLTGTRS DAAVFAFYPN
KQITTGEGGM VVTNRDDLAG LLRSMRNQGR DEGAAWYEHN RLGFNYRMDE MSAALGRVQL
DRLPEILAKR EWVAGKYTEK LDSLAGVSVP GVNPAVQMSW FVYVVRLDPK IDRELVIAEL
ASRNIGSRGY FRPIHLQPFF RKTFGYKPGD FPVAEAAGAS TLALPFYTNM PEEQIDYVVS
NLGDILGRF
//
