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
