ID A4CLB3_ROBBH Unreviewed; 294 AA.
AC A4CLB3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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 OrderedLocusNames=RB2501_15079 {ECO:0000313|EMBL:EAR15662.1};
OS Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Robiginitalea.
OX NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR15662.1, ECO:0000313|Proteomes:UP000009049};
RN [1] {ECO:0000313|EMBL:EAR15662.1, ECO:0000313|Proteomes:UP000009049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC {ECO:0000313|Proteomes:UP000009049};
RX PubMed=19767438; DOI=10.1128/JB.01191-09;
RA Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL J. Bacteriol. 191:7144-7145(2009).
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|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 -!- 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 ECO:0000256|RuleBase:RU003985}.
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DR EMBL; CP001712; EAR15662.1; -; Genomic_DNA.
DR RefSeq; WP_015754978.1; NC_013222.1.
DR AlphaFoldDB; A4CLB3; -.
DR STRING; 313596.RB2501_15079; -.
DR KEGG; rbi:RB2501_15079; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_10; -.
DR OrthoDB; 9808024at2; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000009049; Chromosome.
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; IPR005858; CysM.
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 NCBIfam; TIGR01138; cysM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF162; CYSTEINE SYNTHASE B; 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:UP000009049};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT DOMAIN 6..282
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 72
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 175..179
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 256
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 42
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 294 AA; 32221 MW; DF49D3A80DF2BB7F CRC64;
MPGSLEDLIG NTPLVRSRKL VENPDVALYF KLEGQNPGGS VKDRAALNMI RSMLSRGEIG
PETRLIEATS GNTGIALAMI ARLYNLDLEL VMPANATAER VQTMRAYGAK VTLTPQDVGI
EGARDYAEEK VRDAGYKMFD QFANPDNWKA HYQTTGPEIW RDTRGAITHF VSSMGTTGTI
MGTSAYLKEK NPDIQIVGVQ PDDQASIPGI RKWPQAYLPK IYRPERVDHI LEVTEKEARD
MARRLASEEG IFAGMSSGGA AAAAVRLASE LDSGHIVSIV CDRGDRYLSS DLFE
//
