(data stored in ACNUC29543 zone)

SWISSPROT: A5GQL1_SYNR3

ID   A5GQL1_SYNR3            Unreviewed;       313 AA.
AC   A5GQL1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN   Name=cysK {ECO:0000313|EMBL:CAK27170.1};
GN   OrderedLocusNames=SynRCC307_0267 {ECO:0000313|EMBL:CAK27170.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27170.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27170.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) 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; CT978603; CAK27170.1; -; Genomic_DNA.
DR   RefSeq; WP_011934685.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0267; -.
DR   EnsemblBacteria; CAK27170; CAK27170; SynRCC307_0267.
DR   KEGG; syr:SynRCC307_0267; -.
DR   eggNOG; ENOG4105C6T; Bacteria.
DR   eggNOG; COG0031; LUCA.
DR   HOGENOM; HOG000217394; -.
DR   KO; K01738; -.
DR   OMA; WDSGERY; -.
DR   OrthoDB; 1033353at2; -.
DR   BioCyc; SSP316278:G1GJL-264-MONOMER; -.
DR   Proteomes; UP000001115; 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; A5GQL1.
DR   SWISS-2DPAGE; A5GQL1.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cysteine biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW   ECO:0000256|RuleBase:RU003985};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Transferase {ECO:0000256|RuleBase:RU003985,
KW   ECO:0000313|EMBL:CAK27170.1}.
FT   DOMAIN        8    295       PALP. {ECO:0000259|Pfam:PF00291}.
FT   REGION      181    185       Pyridoxal phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR605856-50}.
FT   BINDING      77     77       Pyridoxal phosphate. {ECO:0000256|PIRSR:
FT                                PIRSR605856-50}.
FT   BINDING     269    269       Pyridoxal phosphate. {ECO:0000256|PIRSR:
FT                                PIRSR605856-50}.
FT   MOD_RES      46     46       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR605856-51}.
SQ   SEQUENCE   313 AA;  33018 MW;  11682A3C9E317298 CRC64;
     MAIAPDITTL VGRTPLVRLN RLPAEENCKA EIVAKLESFN PTASVKDRIG VAMIRDAEAA
     GRIAPDRTVL VEPTSGNTGI ALAMVAAARG YRLILIMPDT MSTERRSMLR AYGAELELTP
     GSEGMKGAIS RARELADELP NAYLLQQFSN SANPAIHAAT TAEELWSDTE GRIDALVAGV
     GTGGTITGCS EVLKQRKPSF QAFAVEPTGS PVLSGGPPGP HRIQGIGAGF VPDNYQPSLV
     DEVLQVDDAE AMVMGRRLAR VEGLLSGVSS GAAMAAALKL GQRPEMEGKL IVVVLASFGE
     RYLSTPMFTE IGF
//

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