位置:首页 > 蛋白库 > CDR_STAA3
CDR_STAA3
ID   CDR_STAA3               Reviewed;         438 AA.
AC   Q2FIA5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Coenzyme A disulfide reductase {ECO:0000255|HAMAP-Rule:MF_01608};
DE            Short=CoA-disulfide reductase {ECO:0000255|HAMAP-Rule:MF_01608};
DE            Short=CoADR {ECO:0000255|HAMAP-Rule:MF_01608};
DE            EC=1.8.1.14 {ECO:0000255|HAMAP-Rule:MF_01608};
GN   Name=cdr {ECO:0000255|HAMAP-Rule:MF_01608};
GN   OrderedLocusNames=SAUSA300_0873;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
CC   -!- FUNCTION: Catalyzes specifically the NADPH-dependent reduction of
CC       coenzyme A disulfide. {ECO:0000255|HAMAP-Rule:MF_01608}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 CoA + NADP(+) = CoA-disulfide + H(+) + NADPH;
CC         Xref=Rhea:RHEA:14705, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62209; EC=1.8.1.14;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01608};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01608};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01608};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01608}.
CC   -!- DOMAIN: Contains 2 FAD binding domains and a single NADPH binding
CC       domain. {ECO:0000255|HAMAP-Rule:MF_01608}.
CC   -!- MISCELLANEOUS: Reduction of disulfides occurs by a thiol-disulfide
CC       exchange reaction, but involves only a single catalytic cysteine
CC       residue that forms a stable mixed disulfide with CoA during catalysis.
CC       {ECO:0000255|HAMAP-Rule:MF_01608}.
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000255|HAMAP-Rule:MF_01608}.
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; CP000255; ABD21541.1; -; Genomic_DNA.
DR   RefSeq; WP_001124525.1; NZ_CP027476.1.
DR   PDB; 4EM3; X-ray; 1.98 A; A/B=2-438.
DR   PDB; 4EM4; X-ray; 1.82 A; A/B=2-438.
DR   PDB; 4EMW; X-ray; 2.39 A; A/B=2-437.
DR   PDB; 4EQR; X-ray; 1.80 A; A/B=2-438.
DR   PDB; 4EQS; X-ray; 1.50 A; A/B=2-438.
DR   PDB; 4EQW; X-ray; 1.50 A; A/B=2-438.
DR   PDB; 4EQX; X-ray; 1.70 A; A/B=2-438.
DR   PDBsum; 4EM3; -.
DR   PDBsum; 4EM4; -.
DR   PDBsum; 4EMW; -.
DR   PDBsum; 4EQR; -.
DR   PDBsum; 4EQS; -.
DR   PDBsum; 4EQW; -.
DR   PDBsum; 4EQX; -.
DR   AlphaFoldDB; Q2FIA5; -.
DR   SMR; Q2FIA5; -.
DR   EnsemblBacteria; ABD21541; ABD21541; SAUSA300_0873.
DR   KEGG; saa:SAUSA300_0873; -.
DR   HOGENOM; CLU_003291_1_3_9; -.
DR   OMA; DKNHTNY; -.
DR   BRENDA; 1.8.1.14; 3352.
DR   Proteomes; UP000001939; Chromosome.
DR   GO; GO:0050451; F:CoA-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_01608; CoA_diS_reduct; 1.
DR   InterPro; IPR017758; CoA_disulphide_reductase.
DR   InterPro; IPR023536; CoA_disulphide_reductase_staph.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR03385; CoA_CoA_reduc; 1.
PE   1: Evidence at protein level;
KW   3D-structure; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
FT   CHAIN           1..438
FT                   /note="Coenzyme A disulfide reductase"
FT                   /id="PRO_0000289961"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   ACT_SITE        43
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         8..33
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         151..166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         267..277
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         419
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           13..23
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          29..36
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           45..49
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           64..71
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          79..85
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   TURN            86..89
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   TURN            96..99
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:4EM3"
FT   HELIX           133..146
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           158..170
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          173..181
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           189..192
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           193..201
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          212..216
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          219..222
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          231..235
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          239..242
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          279..290
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           295..310
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          324..328
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          331..338
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           340..345
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          348..358
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          362..364
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          367..375
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   TURN            376..378
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   STRAND          380..391
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           392..404
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           409..414
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   TURN            421..423
FT                   /evidence="ECO:0007829|PDB:4EQS"
FT   HELIX           429..435
FT                   /evidence="ECO:0007829|PDB:4EQS"
SQ   SEQUENCE   438 AA;  49290 MW;  648B6AFDEFD440F8 CRC64;
     MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRRYAL
     AYTPEKFYDR KQITVKTYHE VIAINDERQT VSVLNRKTNE QFEESYDKLI LSPGASANSL
     GFESDITFTL RNLEDTDAID QFIKANQVDK VLVVGAGYVS LEVLENLYER GLHPTLIHRS
     DKINKLMDAD MNQPILDELD KREIPYRLNE EINAINGNEI TFKSGKVEHY DMIIEGVGTH
     PNSKFIESSN IKLDRKGFIP VNDKFETNVP NIYAIGDIAT SHYRHVDLPA SVPLAWGAHR
     AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM VEVTQGAHAN
     YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GADKRIDVLS MAMMNQLTVD ELTEFEVAYA
     PPYSHPKDLI NMIGYKAK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024