(data stored in SCRATCH zone)

SWISSPROT: D6ZB30_SEGRD

ID   D6ZB30_SEGRD            Unreviewed;       311 AA.
AC   D6ZB30;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 53.
DE   RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN   OrderedLocusNames=Srot_0302 {ECO:0000313|EMBL:ADG96789.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96789.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96789.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG96789.1; -; Genomic_DNA.
DR   RefSeq; WP_013137245.1; NC_014168.1.
DR   STRING; 640132.Srot_0302; -.
DR   EnsemblBacteria; ADG96789; ADG96789; Srot_0302.
DR   KEGG; srt:Srot_0302; -.
DR   eggNOG; ENOG4105C6T; Bacteria.
DR   eggNOG; COG0031; LUCA.
DR   HOGENOM; HOG000217393; -.
DR   KO; K01738; -.
DR   OMA; WDSGERY; -.
DR   OrthoDB; 1033353at2; -.
DR   BioCyc; SROT640132:G1GLH-304-MONOMER; -.
DR   Proteomes; UP000002247; 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; D6ZB30.
DR   SWISS-2DPAGE; D6ZB30.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
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:UP000002247};
KW   Transferase {ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN        9    295       PALP. {ECO:0000259|Pfam:PF00291}.
FT   REGION      179    183       Pyridoxal phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR605856-50}.
FT   BINDING      75     75       Pyridoxal phosphate. {ECO:0000256|PIRSR:
FT                                PIRSR605856-50}.
FT   BINDING     267    267       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   311 AA;  32462 MW;  BE1379FCC5A2C476 CRC64;
     MSKIYENVSD LVGHTPLVQL NRLTAGLPGR VVAKLEYYNP ANSVKDRVGV AIIDAAERSG
     ELRPGGTIVE ATSGNTGIAL AMVGAARGYK VILTMPDTMS VERRAMLRAF GAEIVLTPGS
     EGMAGAVERA KQIIAGTHNA VAANQFSNPA NPAMHEQTTG EEIWADTDGA VDVFVAGIGT
     GGTISGVGRA LKARKPGVRI VGVEPKDSPI LNGGAAGAHK IQGIGANFIP EVLDRDIYDE
     ILDVEFADAI KVARALGVEE GILGGISAGA NVWAALELAK RPENAGKLIV TVVCDFGERY
     ISTALFDHIR D
//

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