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RUBR_DESVH
ID   RUBR_DESVH              Reviewed;          52 AA.
AC   P00269;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Rubredoxin;
DE            Short=Rd;
GN   Name=rub; OrderedLocusNames=DVU_3184;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2549009; DOI=10.1128/jb.171.9.4996-5004.1989;
RA   Brumlik M.J., Voordouw G.;
RT   "Analysis of the transcriptional unit encoding the genes for rubredoxin
RT   (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio
RT   vulgaris Hildenborough.";
RL   J. Bacteriol. 171:4996-5004(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2843442; DOI=10.1016/0378-1119(88)90010-8;
RA   Voordouw G.;
RT   "Cloning of genes encoding redox proteins of known amino acid sequence from
RT   a library of the Desulfovibrio vulgaris (Hildenborough) genome.";
RL   Gene 67:75-83(1988).
RN   [3]
RP   PROTEIN SEQUENCE.
RX   PubMed=7308; DOI=10.1016/0005-2795(76)90030-1;
RA   Bruschi M.;
RT   "Non-heme iron proteins. The amino acid sequence of rubredoxin from
RT   Desulfovibrio vulgaris.";
RL   Biochim. Biophys. Acta 434:4-17(1976).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
RX   PubMed=881725; DOI=10.1016/s0022-2836(77)80159-9;
RA   Adman E.T., Sieker L.C., Jensen L.H., Bruschi M., le Gall J.;
RT   "A structural model of rubredoxin from Desulfovibrio vulgaris at 2-A
RT   resolution.";
RL   J. Mol. Biol. 112:113-120(1977).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=1992166; DOI=10.1016/0022-2836(91)90547-j;
RA   Adman E.T., Seiker L.C., Jensen L.H.;
RT   "Structure of rubredoxin from Desulfovibrio vulgaris at 1.5-A resolution.";
RL   J. Mol. Biol. 217:337-352(1991).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (0.92 ANGSTROMS).
RA   Dauter Z., Butterworth S., Sieker L.C., Sheldrick G., Wilson K.S.;
RL   Submitted (DEC-1997) to the PDB data bank.
CC   -!- FUNCTION: Rubredoxin is a small nonheme, iron protein lacking acid-
CC       labile sulfide. Its single Fe, chelated to 4 Cys, functions as an
CC       electron acceptor and may also stabilize the conformation of the
CC       molecule.
CC   -!- FUNCTION: Electron acceptor for cytoplasmic lactate dehydrogenase.
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC       Note=Binds 1 Fe(3+) ion per subunit.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}.
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DR   EMBL; M28848; AAA64798.1; -; Genomic_DNA.
DR   EMBL; M21679; AAA21088.1; -; Genomic_DNA.
DR   EMBL; M81168; AAA23381.1; -; Genomic_DNA.
DR   EMBL; AE017285; AAS97654.1; -; Genomic_DNA.
DR   PIR; B33962; RUDV.
DR   RefSeq; WP_010940442.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_012394.1; NC_002937.3.
DR   PDB; 1RB9; X-ray; 0.92 A; A=1-52.
DR   PDB; 2KKD; NMR; -; A=1-52.
DR   PDB; 2QL0; NMR; -; A=1-52.
DR   PDB; 7RXN; X-ray; 1.50 A; A=1-52.
DR   PDB; 8RXN; X-ray; 1.00 A; A=1-52.
DR   PDBsum; 1RB9; -.
DR   PDBsum; 2KKD; -.
DR   PDBsum; 2QL0; -.
DR   PDBsum; 7RXN; -.
DR   PDBsum; 8RXN; -.
DR   AlphaFoldDB; P00269; -.
DR   BMRB; P00269; -.
DR   SMR; P00269; -.
DR   STRING; 882.DVU_3184; -.
DR   DrugBank; DB04464; N-Formylmethionine.
DR   PaxDb; P00269; -.
DR   EnsemblBacteria; AAS97654; AAS97654; DVU_3184.
DR   KEGG; dvu:DVU_3184; -.
DR   PATRIC; fig|882.5.peg.2889; -.
DR   eggNOG; COG1773; Bacteria.
DR   HOGENOM; CLU_128747_3_3_7; -.
DR   OMA; APKDMFE; -.
DR   PhylomeDB; P00269; -.
DR   EvolutionaryTrace; P00269; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   CDD; cd00730; rubredoxin; 1.
DR   InterPro; IPR024922; Rubredoxin.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR024935; Rubredoxin_dom.
DR   InterPro; IPR018527; Rubredoxin_Fe_BS.
DR   Pfam; PF00301; Rubredoxin; 1.
DR   PIRSF; PIRSF000071; Rubredoxin; 1.
DR   PRINTS; PR00163; RUBREDOXIN.
DR   PROSITE; PS00202; RUBREDOXIN; 1.
DR   PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Electron transport;
KW   Iron; Metal-binding; Reference proteome; Transport.
FT   CHAIN           1..52
FT                   /note="Rubredoxin"
FT                   /id="PRO_0000135038"
FT   DOMAIN          1..52
FT                   /note="Rubredoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         6
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT                   ECO:0000269|PubMed:7308"
FT   BINDING         9
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT                   ECO:0000269|PubMed:7308"
FT   BINDING         39
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT                   ECO:0000269|PubMed:7308"
FT   BINDING         42
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241,
FT                   ECO:0000269|PubMed:7308"
FT   CONFLICT        21
FT                   /note="D -> T (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:1RB9"
FT   TURN            7..9
FT                   /evidence="ECO:0007829|PDB:1RB9"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:1RB9"
FT   HELIX           20..22
FT                   /evidence="ECO:0007829|PDB:1RB9"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:1RB9"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1RB9"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:1RB9"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:1RB9"
SQ   SEQUENCE   52 AA;  5574 MW;  656BC412F3E1B8CC CRC64;
     MKKYVCTVCG YEYDPAEGDP DNGVKPGTSF DDLPADWVCP VCGAPKSEFE AA
 
 
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