(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHM4_GEOS0

ID   A0A0F6BHM4_GEOS0        Unreviewed;       308 AA.
AC   A0A0F6BHM4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 22.
DE   RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN   OrderedLocusNames=GY4MC1_0069 {ECO:0000313|EMBL:ADP72925.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72925.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72925.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72925.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-
CC         cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340;
CC         EC=2.5.1.47; Evidence={ECO:0000256|RuleBase:RU003985};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR605856-50,
CC         ECO:0000256|RuleBase:RU003985};
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|RuleBase:RU003985}.
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DR   EMBL; CP002293; ADP72925.1; -; Genomic_DNA.
DR   RefSeq; WP_003247476.1; NC_014650.1.
DR   EnsemblBacteria; ADP72925; ADP72925; GY4MC1_0069.
DR   GeneID; 29237309; -.
DR   KEGG; gmc:GY4MC1_0069; -.
DR   KO; K01738; -.
DR   OMA; WDSGERY; -.
DR   OrthoDB; 1033353at2; -.
DR   BioCyc; GSP581103:G1GOQ-82-MONOMER; -.
DR   Proteomes; UP000002034; 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   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01139; cysK; 1.
DR   TIGRFAMs; TIGR01136; cysKM; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHM4.
DR   SWISS-2DPAGE; A0A0F6BHM4.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cysteine biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW   ECO:0000256|RuleBase:RU003985};
KW   Transferase {ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN        9    292       PALP. {ECO:0000259|Pfam:PF00291}.
FT   REGION      178    182       Pyridoxal phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR605856-50}.
FT   BINDING      75     75       Pyridoxal phosphate. {ECO:0000256|PIRSR:
FT                                PIRSR605856-50}.
FT   BINDING     266    266       Pyridoxal phosphate. {ECO:0000256|PIRSR:
FT                                PIRSR605856-50}.
FT   MOD_RES      45     45       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR605856-51}.
SQ   SEQUENCE   308 AA;  32647 MW;  5818FFDC47A2B865 CRC64;
     MARTVNSVTE LIGDTPAVKL NRIVDEDSAD VYLKLEFMNP GSSVKDRIAL AMIEAAEKEG
     KIKPGDTIVE PTSGNTGIGL AMVAAAKGYK AILVMPDTMS LERRNLLRAY GAELVLTPGS
     QGMRGAIAKA EELVKEHGYF MPQQFKNEAN PEIHRLTTGK EIVEQMGDQL DAFIAGVGTG
     GTITGAGQVL REKYPNIKIY AVEPADSPVL SGGKPGPHKI QGIGAGFVPD ILDTSIYDGV
     ITVTTEEAFA AARRAAREEG ILGGISSGAA IHAALKIAKQ LGKGKKVLAI IPSNGERYLS
     TPLYQFDE
//

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