ID W4V556_9FIRM Unreviewed; 302 AA.
AC W4V556;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=O-acetylserine (thiol)-lyase {ECO:0000256|ARBA:ARBA00030296};
GN ORFNames=JCM21531_1313 {ECO:0000313|EMBL:GAE87908.1};
OS Acetivibrio straminisolvens JCM 21531.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE87908.1, ECO:0000313|Proteomes:UP000019109};
RN [1] {ECO:0000313|EMBL:GAE87908.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE87908.1};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT Isolated from a Cellulose-Degrading Bacterial Community.";
RL Genome Announc. 2:e00110-14(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR605856-50};
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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:GAE87908.1}.
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; BAVR01000011; GAE87908.1; -; Genomic_DNA.
DR RefSeq; WP_038287777.1; NZ_BAVR01000011.1.
DR AlphaFoldDB; W4V556; -.
DR STRING; 1294263.JCM21531_1313; -.
DR OrthoDB; 9808024at2; -.
DR Proteomes; UP000019109; Unassembled WGS sequence.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:InterPro.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR005856; Cys_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01136; cysKM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF211; PALP DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR605856-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000019109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..290
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 73
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 177..181
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 264
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 43
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 302 AA; 32754 MW; EBEB914B74DE0E63 CRC64;
MKYDDMQQLI GNTPLVRLRH SGFPDGVRVY AKLELYNPSG SVKDRIGKYM IEDAEKRGIL
VPGSTIVEGT AGNTGLGIAF AALNRGYRLI MVVPTKFSQE KQALLRALGA EVINTPREEG
MLGAERKAEE LRQSIPKAVS LEQFRNPSNP LAHYETTGPE IWTDLGADID YFVAGAGSGG
TYAGIVRYLK EQKRDIKGIL ADPIGSTMGG GEHGDYDIEG IGNDFIPDTM DMSLVDDVIK
VSDDEAFAEA RLLARNEGII AGSSSGANLA AVRKLAMRIQ CGTIVTVLPD RGERYLSKNL
FL
//
