HMP_DEIRA
ID HMP_DEIRA Reviewed; 403 AA.
AC Q9RYR5;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Flavohemoprotein {ECO:0000255|HAMAP-Rule:MF_01252};
DE AltName: Full=Flavohemoglobin {ECO:0000255|HAMAP-Rule:MF_01252};
DE AltName: Full=Hemoglobin-like protein {ECO:0000255|HAMAP-Rule:MF_01252};
DE AltName: Full=Nitric oxide dioxygenase {ECO:0000255|HAMAP-Rule:MF_01252};
DE Short=NO oxygenase {ECO:0000255|HAMAP-Rule:MF_01252};
DE Short=NOD {ECO:0000255|HAMAP-Rule:MF_01252};
DE EC=1.14.12.17 {ECO:0000255|HAMAP-Rule:MF_01252};
GN Name=hmp {ECO:0000255|HAMAP-Rule:MF_01252}; OrderedLocusNames=DR_A0243;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01252};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01252};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01252};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01252};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01252};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01252};
CC -!- DOMAIN: Consists of two distinct domains; an 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|HAMAP-Rule:MF_01252}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01252}.
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DR EMBL; AE001825; AAF12394.1; -; Genomic_DNA.
DR PIR; D75577; D75577.
DR RefSeq; NP_285566.1; NC_001264.1.
DR RefSeq; WP_010889502.1; NZ_CP015082.1.
DR AlphaFoldDB; Q9RYR5; -.
DR SMR; Q9RYR5; -.
DR STRING; 243230.DR_A0243; -.
DR EnsemblBacteria; AAF12394; AAF12394; DR_A0243.
DR KEGG; dra:DR_A0243; -.
DR PATRIC; fig|243230.17.peg.3133; -.
DR eggNOG; COG1017; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_12_0_0; -.
DR InParanoid; Q9RYR5; -.
DR OMA; ADIHYEV; -.
DR OrthoDB; 1834577at2; -.
DR Proteomes; UP000002524; Chromosome II.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IBA:GO_Central.
DR GO; GO:0046210; P:nitric oxide catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_01252; Hmp; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR000951; Ph_dOase_redase.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43396:SF3; PTHR43396:SF3; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase;
KW Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..403
FT /note="Flavohemoprotein"
FT /id="PRO_0000052430"
FT DOMAIN 152..257
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT REGION 1..138
FT /note="Globin"
FT REGION 149..403
FT /note="Reductase"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT BINDING 85
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|HAMAP-Rule:MF_01252"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT BINDING 206..209
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT BINDING 269..274
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT BINDING 390..393
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT SITE 29
FT /note="Involved in heme-bound ligand stabilization and O-O
FT bond activation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT SITE 84
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT SITE 389
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
SQ SEQUENCE 403 AA; 43296 MW; 7402654E60039312 CRC64;
MLTPEQKAIV KATVPALEAH GETITRTFYA SMFAAHPELL NIFNPANQQT GKQARSLAAS
VLAYAAHIDH PEALGGMVGR IAHKHVSLEV LPEHYPIVGQ YLLGAIAGVL GDAAKPEILD
AWAAAYGELA DLMIGIEKGM YDAGAGQPGG WRDFRPFRVA RKVAESRVIT SFVLEPVGGG
ALPAYQPGQY LSLKVKVPGQ ERWQIRQYSL SDAPSPDHYR ISVKREGGGL VSEYLHGAVQ
EGDELLVHVP AGDFVLQQSE RPVVLISAGV GITPMLAMVQ TLAQAGSQRP VTFIHAAQNG
SVHAFRDDVA RLTHEYPHFR KVVFYDEAGP DDQLGTHHDV AGRLSLDAVR GALPAGEAEF
YYCGPAGFAG AVEAILDDLQ VPAERRFTET FGPSQSFAPV ILG
