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FHP_CANNO
ID   FHP_CANNO               Reviewed;         390 AA.
AC   Q03331;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 3.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Flavohemoprotein;
DE            EC=1.14.12.17;
DE   AltName: Full=Flavohemoglobin;
DE   AltName: Full=Hemoglobin-like protein;
DE   AltName: Full=Nitric oxide dioxygenase;
DE            Short=NO oxygenase;
DE            Short=NOD;
OS   Candida norvegensis (Yeast) (Candida mycoderma).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT
RP   SER-2.
RC   STRAIN=NBRC 0734 / CBS 6917 / SIFF V-342a;
RX   PubMed=1404399; DOI=10.1016/0022-2836(92)90236-d;
RA   Iwaasa H., Takagi T., Shikama K.;
RT   "Amino acid sequence of yeast hemoglobin. A two-domain structure.";
RL   J. Mol. Biol. 227:948-954(1992).
RN   [2]
RP   SEQUENCE REVISION TO 389-390.
RA   Takagi T.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   COFACTOR.
RX   PubMed=4798061; DOI=10.1111/j.1432-1033.1973.tb03157.x;
RA   Oshino R., Asakura T., Takio K., Oshino N., Chance B., Hagihara B.;
RT   "Purification and molecular properties of yeast hemoglobin.";
RL   Eur. J. Biochem. 39:581-590(1973).
RN   [4]
RP   ABSORPTION SPECTROSCOPY, AND CIRCULAR DICHROISM ANALYSIS.
RX   PubMed=12192008; DOI=10.1074/jbc.m206529200;
RA   Kobayashi G., Nakamura T., Ohmachi H., Matsuoka A., Ochiai T., Shikama K.;
RT   "Yeast flavohemoglobin from Candida norvegensis. Its structural, spectral,
RT   and stability properties.";
RL   J. Biol. Chem. 277:42540-42548(2002).
RN   [5]
RP   REVIEW.
RX   PubMed=7584595; DOI=10.1016/1357-2725(95)00084-3;
RA   Shikama K., Matsuoka A., Iwaasa H.;
RT   "The unique structures of protozoan myoglobin and yeast hemoglobin: an
RT   evolutionary diversity.";
RL   Int. J. Biochem. Cell Biol. 27:1107-1115(1995).
CC   -!- FUNCTION: Is involved in NO detoxification in an aerobic process,
CC       termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and
CC       NAD(P)H to convert NO to nitrate, which protects the fungus from
CC       various noxious nitrogen compounds. Therefore, plays a central role in
CC       the inducible response to nitrosative stress (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: In the presence of oxygen and NADH, it has NADH oxidase
CC       activity, which leads to the generation of superoxide and H(2)O(2).
CC       Under anaerobic conditions, it also exhibits nitric oxide reductase and
CC       FAD reductase activities. However, all these reactions are much lower
CC       than NOD activity (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate;
CC         Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.14.12.17;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate;
CC         Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.14.12.17;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:4798061};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:4798061};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000269|PubMed:4798061};
CC       Note=Binds 1 heme b group per subunit. {ECO:0000269|PubMed:4798061};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Consists of two distinct domains; a N-terminal heme-containing
CC       oxygen-binding domain and a C-terminal reductase domain with binding
CC       sites for FAD and NAD(P)H.
CC   -!- SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00238}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family. {ECO:0000305}.
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DR   EMBL; X68849; CAA48729.2; -; mRNA.
DR   PIR; S26964; S26964.
DR   AlphaFoldDB; Q03331; -.
DR   SMR; Q03331; -.
DR   iPTMnet; Q03331; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008941; F:nitric oxide dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0051409; P:response to nitrosative stress; IEA:InterPro.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.490.10; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR023950; Hmp.
DR   InterPro; IPR000951; Ph_dOase_redase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43396:SF3; PTHR43396:SF3; 1.
DR   Pfam; PF00042; Globin; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Detoxification; Direct protein sequencing; FAD;
KW   Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1404399"
FT   CHAIN           2..390
FT                   /note="Flavohemoprotein"
FT                   /id="PRO_0000052459"
FT   DOMAIN          158..263
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          10..151
FT                   /note="Globin"
FT   REGION          157..390
FT                   /note="Reductase"
FT   ACT_SITE        106
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         196
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         214..217
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         277..282
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         382..385
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   SITE            40
FT                   /note="Involved in heme-bound ligand stabilization and O-O
FT                   bond activation"
FT                   /evidence="ECO:0000250"
FT   SITE            95
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000250"
FT   SITE            381
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1404399"
SQ   SEQUENCE   390 AA;  44363 MW;  8066E37384A15ED4 CRC64;
     MSAAKQLFKI VPLTPTEINF LQSLAPVVKE HGVTVTSTMY KYMFQTYPEV RSYFNMTNQK
     TGRQPKVLAF SLYQYILHLN DLTPISGFVN QIVLKHCGLG IKPDQYPVVG ESLVQAFKMV
     LGEAADEHFV EVFKKAYGNL AQTLIDAEAS VYKTLAWEEF KDFRVTKLVK EAEDVTSVYL
     TPVDGFKLKP IIPGEYISFR WDIHNPDITD IQPREYSISQ DVKENEYRIS VRDIGIVSDY
     INKKLQVGDI VPVHAPVGTM KYDSISKKGK VAVLAGGIGI TPMIPIIEHA LKDGKDVELY
     YSNRSYQSEP FREFFSNLEK ENNGKFKLNN YISAENQKLQ VKDLEHINPD EYDVYLLGPV
     AYMHEFKTYL VGKGVSDLKM EFFGPTDPDC
 
 
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