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Database: UniProt
Entry: W6M5H8_9GAMM
LinkDB: W6M5H8_9GAMM
Original site: W6M5H8_9GAMM 
ID   W6M5H8_9GAMM            Unreviewed;       335 AA.
AC   W6M5H8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   Name=cysM {ECO:0000313|EMBL:CDI01025.1};
GN   ORFNames=BN873_100037 {ECO:0000313|EMBL:CDI01025.1};
OS   Candidatus Competibacter denitrificans Run_A_D11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria;
OC   Candidatus Competibacteraceae; Candidatus Competibacter.
OX   NCBI_TaxID=1400863 {ECO:0000313|EMBL:CDI01025.1, ECO:0000313|Proteomes:UP000035760};
RN   [1] {ECO:0000313|EMBL:CDI01025.1, ECO:0000313|Proteomes:UP000035760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI01025.1,
RC   ECO:0000313|Proteomes:UP000035760};
RA   McIlroy S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDI01025.1, ECO:0000313|Proteomes:UP000035760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI01025.1,
RC   ECO:0000313|Proteomes:UP000035760};
RA   McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., Kristiansen R.,
RA   Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.;
RT   "Candidatus Competibacter-lineage genomes retrieved from metagenomes reveal
RT   functional metabolic diversity.";
RL   Submitted (FEB-2014) 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   -!- 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}.
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:CDI01025.1}.
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DR   EMBL; CBTJ020000002; CDI01025.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6M5H8; -.
DR   STRING; 1400863.BN873_100037; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000035760; Unassembled WGS sequence.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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}; Hydrolase {ECO:0000313|EMBL:CDI01025.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR605856-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          47..322
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         112
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         215..219
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         296
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         82
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   335 AA;  35966 MW;  162658E48A424941 CRC64;
     MLAPAHEILL FVIGLTYFTG RENARSQNFA DNPESTMPHS PYPTLESFVG NTPLIRIQRL
     AVQRDNLLLG KLEGNNPAGS VKDRPALSMI RCAEARGAIR PGDGLIEATS GNTGIALAMI
     AAIKGYRLTL VMPENQSVER RAAMRAYGAE LLLVSQSEGM EGARDLAARL EREGKGKVLD
     QFANPDNPLA HYQTTGPEIW RDTGGKITHF VSAMGTTGTI MGVSRYLKER DPTVQIVGVQ
     PTEGSSIAGI RRWPLAYLPA IFDPARVDQI IDVSQAEAEN TTRRLACEEG ICCGVSSGGA
     VAAALQLADT VENAVIVTIL CDRGDRYLST GLFAA
//
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