位置:首页 > 蛋白库 > CSD_STAAN
CSD_STAAN
ID   CSD_STAAN               Reviewed;         413 AA.
AC   P99177; Q99VG1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=SA0776;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=N315;
RX   PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA   Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA   Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA   Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT   "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT   aureus during the post-exponential phase of growth.";
RL   J. Microbiol. Methods 60:247-257(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC       from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC       produce L-alanine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC         alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64428; EC=2.8.1.7;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000018; BAB42015.1; -; Genomic_DNA.
DR   PIR; D89857; D89857.
DR   AlphaFoldDB; P99177; -.
DR   SMR; P99177; -.
DR   SWISS-2DPAGE; P99177; -.
DR   EnsemblBacteria; BAB42015; BAB42015; BAB42015.
DR   KEGG; sau:SA0776; -.
DR   HOGENOM; CLU_003433_2_5_9; -.
DR   OMA; HKLCGPT; -.
DR   Proteomes; UP000000751; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   CDD; cd06453; SufS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
PE   1: Evidence at protein level;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..413
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150311"
FT   ACT_SITE        368
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  46322 MW;  CE1E87F33391F6D4 CRC64;
     MAEHSFDVNE VIKDFPILDQ KVNGKRLAYL DSTATSQTPM QVLNVLEDYY KRYNSNVHRG
     VHTLGSLATD GYENARETVR RFINAKYFEE IIFTRGTTAS INLVAHSYGD ANVEEGDEIV
     VTEMEHHANI VPWQQLAKRK NATLKFIPMT ADGELNIEDI KQTINDKTKI VAIAHISNVL
     GTINDVKTIA EIAHQHGAII SVDGAQAAPH MKLDMQEMNA DFYSFSGHKM LGPTGIGVLF
     GKRELLQKME PIEFGGDMID FVSKYDATWA DLPTKFEAGT PLIAQAIGLA EAIRYLERIG
     FDAIHKYEQE LTIYAYEQMS AIEGIEIYGP PKDRRAGVIT FNLQDVHPHD VATAVDTEGV
     AVRAGHHCAQ PLMKWLNVSS TARASFYIYN TKEDIDQLIN ALKQTKEFFS YEF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024