ID A0A3N0VAB8_9GAMM Unreviewed; 455 AA.
AC A0A3N0VAB8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN ORFNames=ED208_10505 {ECO:0000313|EMBL:ROH89551.1};
OS Stagnimonas aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Stagnimonas.
OX NCBI_TaxID=2689987 {ECO:0000313|EMBL:ROH89551.1, ECO:0000313|Proteomes:UP000282106};
RN [1] {ECO:0000313|EMBL:ROH89551.1, ECO:0000313|Proteomes:UP000282106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=THS-13 {ECO:0000313|EMBL:ROH89551.1,
RC ECO:0000313|Proteomes:UP000282106};
RA Chen W.-M.;
RL Submitted (OCT-2018) 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}.
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:ROH89551.1}.
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DR EMBL; RJVO01000004; ROH89551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0VAB8; -.
DR InParanoid; A0A3N0VAB8; -.
DR Proteomes; UP000282106; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProt.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR CDD; cd04608; CBS_pair_CBS; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR046353; CBS_C.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF191; CYSTATHIONINE BETA-SYNTHASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00291; PALP; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000282106}.
FT DOMAIN 335..397
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 455 AA; 49477 MW; 365208F688F566CB CRC64;
MRRDGRVLDT IGNTPLVELK NLDSGPCRLF VKLENQNPTG SIKDRIGLSM IEAAEREGRI
QPGGRLVEAT AGNTGLGLAL VAAQKGYRLT LVIPDKMAQE KVLHLKALGA EIHITRSDVG
KGHPEYYQDI AERLARETGA FYVNQFANPA NPYAHEATTG PEIWAQSQQM LDAVVVGVGS
GGTLTGLSRY FARVAPHVEM VLADPKGSIL VDVVKTGTIQ KEAGSWLVEG IGEDFIPPNC
DLARVKAAYE IPDAESFFTA RELLAKEGIL GGSSTGTLLA AALRYCREQT APKRVVSFVC
DSGNKYLSKM YNDFWMFEQG LLERPSHGNL LDLIVRRYAE GSAVTVRPED TLLHAYRRMK
LFDVSQLPVM EGDAVVGILD ESDLLLQVHA DPARFKEPVS AAMSREVVTI APGAPVAELL
PIFAKDLVAV VAEAGRFVGL ITKIDLLNYL RKQLG
//
