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Database: UniProt
Entry: A0A0M8MP76_9MICO
LinkDB: A0A0M8MP76_9MICO
Original site: A0A0M8MP76_9MICO 
ID   A0A0M8MP76_9MICO        Unreviewed;       326 AA.
AC   A0A0M8MP76;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=XI38_07135 {ECO:0000313|EMBL:KOS11040.1};
OS   Microbacterium chocolatum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=84292 {ECO:0000313|EMBL:KOS11040.1, ECO:0000313|Proteomes:UP000037737};
RN   [1] {ECO:0000313|EMBL:KOS11040.1, ECO:0000313|Proteomes:UP000037737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIT 101 {ECO:0000313|EMBL:KOS11040.1,
RC   ECO:0000313|Proteomes:UP000037737};
RA   Li X., Xu Y.;
RT   "Complete genome sequence of Microbacterium chocolatum SIT 101, a bacterium
RT   enantioselectively hydrolyzing mesomeric diesters.";
RL   Submitted (APR-2015) 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:KOS11040.1}.
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DR   EMBL; LAVO01000006; KOS11040.1; -; Genomic_DNA.
DR   RefSeq; WP_053547633.1; NZ_KQ440287.1.
DR   AlphaFoldDB; A0A0M8MP76; -.
DR   KEGG; mcw:A8L33_08030; -.
DR   PATRIC; fig|84292.3.peg.1456; -.
DR   OrthoDB; 9805733at2; -.
DR   Proteomes; UP000037737; 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:UP000037737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          18..305
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         85
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         189..193
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         277
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         55
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   326 AA;  34347 MW;  6624144D612F112F CRC64;
     MTAPAAPVDT PPRIHDDITT AFGGTPLVRL NRLTEGLDAE VVTKLEFYNP GRSVKCRLGI
     ALLDAAEASG ELRPGGTVVE STSGNTGIAL ALAGAARGYR VILTMPASMS KERRTLLKAY
     GAELVLTNPH KGMTEAVETA RRIVAETPGA ILARQFESPA NPEIHRRTTA EEIWRDTDGR
     VDWFVAGSGT GGTLTGVGQA LKERSPALKV VAVEPADSPM LSEGRAGGHR IQGIGPNFVP
     EVLDRSVIDE VMTVGFDEAI DVARALGTRE GILAGMSAGA AVWAALQIAA RPEARGSRIV
     VIVPDSGERY LSTALYAHLR EPAESA
//
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