ID K5CTG9_9BACE Unreviewed; 316 AA.
AC K5CTG9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Cysteine synthase {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
GN ORFNames=HMPREF1057_00008 {ECO:0000313|EMBL:EKJ92710.1};
OS Bacteroides finegoldii CL09T03C10.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997888 {ECO:0000313|EMBL:EKJ92710.1, ECO:0000313|Proteomes:UP000007995};
RN [1] {ECO:0000313|EMBL:EKJ92710.1, ECO:0000313|Proteomes:UP000007995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL09T03C10 {ECO:0000313|EMBL:EKJ92710.1,
RC ECO:0000313|Proteomes:UP000007995};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides finegoldii CL09T03C10.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000256|ARBA:ARBA00000298,
CC ECO:0000256|RuleBase:RU003985};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR605856-50, ECO:0000256|RuleBase:RU003985};
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC ECO:0000256|RuleBase:RU003985}.
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:EKJ92710.1}.
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DR EMBL; AGXW01000001; EKJ92710.1; -; Genomic_DNA.
DR RefSeq; WP_007758469.1; NZ_JH951901.1.
DR AlphaFoldDB; K5CTG9; -.
DR HOGENOM; CLU_021018_1_0_10; -.
DR OrthoDB; 9808024at2; -.
DR Proteomes; UP000007995; Unassembled WGS sequence.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR005856; Cys_synth.
DR InterPro; IPR005859; CysK.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01139; cysK; 1.
DR NCBIfam; TIGR01136; cysKM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 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|RuleBase:RU003985};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW ECO:0000256|RuleBase:RU003985};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR605856-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000007995};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT DOMAIN 9..297
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 77
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 181..185
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 269
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 47
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 316 AA; 33312 MW; 39B31857B6682C4B CRC64;
MAKIAKKLTD LVGNTPLMEL SGYCGKYGLE QNIIAKLEAF NPAGSVKDRV ALSMIEDAEA
RGVLKPGATI IEPTSGNTGV GLAMVATIKG YHLILTMPET MSLERRNLLK ALGAEIVLTD
GLGGMAASIA KAEELRDSIP GSVILQQFEN PANAAAHERT TGEEIWRDTD GEVDVFVAGV
GTGGTVCGVA RALKKHNPDI YIVAVEPAAS PVLEGGQAAP HRIQGIGANF IPKLYDASMI
DEVIGVPDDE AIRAGRELSA TEGLLAGISS GAAVYAARQL AQRPEFKNKK IVALLPDTGE
RYLSTELFAF DAYPLD
//
