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NIGY_DESVH
ID   NIGY_DESVH              Reviewed;         202 AA.
AC   P30820;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 3.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Nigerythrin;
GN   Name=ngr; OrderedLocusNames=DVU_0019;
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=9226272; DOI=10.1128/jb.179.14.4607-4615.1997;
RA   Lumppio H.L., Shenvi N.V., Garg R.P., Summers A.O., Kurtz D.M. Jr.;
RT   "A rubrerythrin operon and nigerythrin gene in Desulfovibrio vulgaris
RT   (Hildenborough).";
RL   J. Bacteriol. 179:4607-4615(1997).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 1-15.
RX   PubMed=8383040; DOI=10.1111/j.1432-1033.1993.tb17655.x;
RA   Pierik A.J., Wolbert R.B.G., Portier G.L., Verhagen M.F.J.M., Hagen W.R.;
RT   "Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two
RT   mononuclear iron centers and two dinuclear iron clusters.";
RL   Eur. J. Biochem. 212:237-245(1993).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS), AND IRON-BINDING SITES.
RX   PubMed=15895271; DOI=10.1007/s00775-005-0650-8;
RA   Iyer R.B., Silaghi-Dumitrescu R., Kurtz D.M. Jr., Lanzilotta W.N.;
RT   "High-resolution crystal structures of Desulfovibrio vulgaris
RT   (Hildenborough) nigerythrin: facile, redox-dependent iron movement, domain
RT   interface variability, and peroxidase activity in the rubrerythrins.";
RL   J. Biol. Inorg. Chem. 10:407-416(2005).
CC   -!- FUNCTION: Exhibits NADH peroxidase activity (in vitro).
CC   -!- SUBUNIT: Homodimer. May possess two rubredoxin-like centers and two
CC       hemerythrin-like binuclear-iron centers per dimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; U71215; AAC45480.1; -; Genomic_DNA.
DR   EMBL; AE017285; AAS94503.1; -; Genomic_DNA.
DR   RefSeq; WP_010937330.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_009244.1; NC_002937.3.
DR   PDB; 1YUX; X-ray; 1.60 A; A/B=1-202.
DR   PDB; 1YUZ; X-ray; 1.40 A; A/B=1-202.
DR   PDB; 1YV1; X-ray; 1.50 A; A/B=1-202.
DR   PDBsum; 1YUX; -.
DR   PDBsum; 1YUZ; -.
DR   PDBsum; 1YV1; -.
DR   AlphaFoldDB; P30820; -.
DR   SMR; P30820; -.
DR   IntAct; P30820; 1.
DR   PaxDb; P30820; -.
DR   EnsemblBacteria; AAS94503; AAS94503; DVU_0019.
DR   KEGG; dvu:DVU_0019; -.
DR   PATRIC; fig|882.5.peg.16; -.
DR   eggNOG; COG1592; Bacteria.
DR   HOGENOM; CLU_095256_1_0_7; -.
DR   OMA; NEVHICS; -.
DR   PhylomeDB; P30820; -.
DR   EvolutionaryTrace; P30820; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd01041; Rubrerythrin; 1.
DR   Gene3D; 1.20.1260.10; -; 1.
DR   InterPro; IPR012347; Ferritin-like.
DR   InterPro; IPR009040; Ferritin-like_diiron.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR003251; Rubrerythrin.
DR   Pfam; PF02915; Rubrerythrin; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 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..202
FT                   /note="Nigerythrin"
FT                   /id="PRO_0000135072"
FT   DOMAIN          23..168
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   DOMAIN          169..202
FT                   /note="Rubredoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT   BINDING         40
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         73
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         73
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         115
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         118
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         152
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   BINDING         174
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT   BINDING         177
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT   BINDING         189
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT   BINDING         192
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT   CONFLICT        129
FT                   /note="K -> E (in Ref. 1; AAC45480)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="E -> G (in Ref. 1; AAC45480)"
FT                   /evidence="ECO:0000305"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   HELIX           29..56
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   HELIX           60..87
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   HELIX           104..120
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   HELIX           122..133
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   HELIX           136..161
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   TURN            190..192
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   HELIX           196..198
FT                   /evidence="ECO:0007829|PDB:1YUZ"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:1YUZ"
SQ   SEQUENCE   202 AA;  22098 MW;  DF5410519EE8D899 CRC64;
     MKVRAQVPTV KNATNFNMVA DSKTAVGSTL ENLKAAIAGE TGAHAKYTAF AKAAREQGYE
     QIARLFEATA AAELIHIGLE YALVAEMEPG YEKPTVAAPS AYSCDLNLIS GANGEIYETS
     DMYPAFIRKA QEEGNSKAVH VFTRAKLAES VHAERYLAAY NDIDAPDDDK FHLCPICGYI
     HKGEDFEKCP ICFRPKDTFT AY
 
 
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