位置:首页 > 蛋白库 > NRFA_VIBPA
NRFA_VIBPA
ID   NRFA_VIBPA              Reviewed;         475 AA.
AC   Q87ND9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Cytochrome c-552 {ECO:0000255|HAMAP-Rule:MF_01182};
DE            EC=1.7.2.2 {ECO:0000255|HAMAP-Rule:MF_01182};
DE   AltName: Full=Ammonia-forming cytochrome c nitrite reductase {ECO:0000255|HAMAP-Rule:MF_01182};
DE            Short=Cytochrome c nitrite reductase {ECO:0000255|HAMAP-Rule:MF_01182};
DE   Flags: Precursor;
GN   Name=nrfA {ECO:0000255|HAMAP-Rule:MF_01182}; OrderedLocusNames=VP1929;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six
CC       electrons in the process. {ECO:0000255|HAMAP-Rule:MF_01182}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6 Fe(III)-[cytochrome c] + 2 H2O + NH4(+) = 6 Fe(II)-
CC         [cytochrome c] + 8 H(+) + nitrite; Xref=Rhea:RHEA:13089, Rhea:RHEA-
CC         COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01182};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01182};
CC       Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01182};
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01182};
CC       Note=Binds 5 heme c groups covalently per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_01182};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC       {ECO:0000255|HAMAP-Rule:MF_01182}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01182}.
CC   -!- SIMILARITY: Belongs to the cytochrome c-552 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01182}.
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; BA000031; BAC60192.1; -; Genomic_DNA.
DR   RefSeq; NP_798308.1; NC_004603.1.
DR   RefSeq; WP_005483164.1; NC_004603.1.
DR   AlphaFoldDB; Q87ND9; -.
DR   SMR; Q87ND9; -.
DR   STRING; 223926.28806921; -.
DR   EnsemblBacteria; BAC60192; BAC60192; BAC60192.
DR   GeneID; 1189436; -.
DR   KEGG; vpa:VP1929; -.
DR   PATRIC; fig|223926.6.peg.1844; -.
DR   eggNOG; COG3303; Bacteria.
DR   HOGENOM; CLU_035040_1_0_6; -.
DR   OMA; EMVILWA; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00548; NrfA-like; 1.
DR   HAMAP; MF_01182; Cytochrom_C552; 1.
DR   InterPro; IPR003321; Cyt_c552.
DR   InterPro; IPR017570; Cyt_c_NO2Rdtase_formate-dep.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   PANTHER; PTHR30633; PTHR30633; 1.
DR   Pfam; PF02335; Cytochrom_C552; 1.
DR   PIRSF; PIRSF000243; Cyt_c552; 1.
DR   SUPFAM; SSF48695; SSF48695; 1.
DR   TIGRFAMs; TIGR03152; cyto_c552_HCOOH; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE   3: Inferred from homology;
KW   Calcium; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase;
KW   Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   CHAIN           30..475
FT                   /note="Cytochrome c-552"
FT                   /id="PRO_0000268982"
FT   REGION          38..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         92
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         120
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         123
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         124
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         158
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         161
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         162
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         207
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         210
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         211
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         259
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         261
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         273
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="5"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         280
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         283
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         284
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         299
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         312
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="5"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         315
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="5"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         316
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="5"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         391
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
SQ   SEQUENCE   475 AA;  53262 MW;  1BB4C5D421A0E797 CRC64;
     MSIKHWMSAP IAVATLFASQ LLLAGSVLAA ENNDRLDPRN DAFEQKHPDQ YHSWKATSES
     KHIEDALSED PNMVILWAGY GFAKDYNKAR GHFYALDDVR QTLRTGAPAD ENSGPMPMAC
     WSCKSPDVAR VIEERGEDGY FSGKWARLGS EIVNPIGCSD CHDTRSEKFN QGEPELALTR
     PYVERAFDVI GKNFDDQSRL DKQASVCAQC HVEYYFTGPT KAVKFPWDMG TTVGDMEKYY
     DALDFKDWTH AVSKAPMLKA QHPGFETWRE GIHGKNKVVC VDCHMPKVTK ADGTVYTDHK
     VGNPFDRFED TCAQCHTQTK EQLRNIVSSR KALVLNMKLT AEKQIVAAHF EAGEAWKAGA
     TEEEMKPILQ DIRHAQWRWD YAIASHGVHM HAPEVALEVL GTAVDRAADA RTKLVRLLAT
     KGITEPVQIP DISTKAKAQE ALGMDMEKMN ADKKHFLDTV VPDWDKAAAE REATY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024