ID A0A0A7KG75_9DEIO Unreviewed; 412 AA.
AC A0A0A7KG75;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Flavohemoprotein {ECO:0000256|HAMAP-Rule:MF_01252};
DE AltName: Full=Flavohemoglobin {ECO:0000256|HAMAP-Rule:MF_01252};
DE AltName: Full=Hemoglobin-like protein {ECO:0000256|HAMAP-Rule:MF_01252};
DE AltName: Full=Nitric oxide dioxygenase {ECO:0000256|HAMAP-Rule:MF_01252};
DE Short=NO oxygenase {ECO:0000256|HAMAP-Rule:MF_01252};
DE Short=NOD {ECO:0000256|HAMAP-Rule:MF_01252};
DE EC=1.14.12.17 {ECO:0000256|HAMAP-Rule:MF_01252};
GN Name=hmp {ECO:0000256|HAMAP-Rule:MF_01252};
GN ORFNames=QR90_08200 {ECO:0000313|EMBL:AIZ45100.1};
OS Deinococcus radiopugnans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ45100.1, ECO:0000313|Proteomes:UP000030634};
RN [1] {ECO:0000313|Proteomes:UP000030634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter sp. DG25B genome submission.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000126, ECO:0000256|HAMAP-
CC Rule:MF_01252};
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 Evidence={ECO:0000256|ARBA:ARBA00001762, ECO:0000256|HAMAP-
CC Rule:MF_01252};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01252};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01252};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01252};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|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. {ECO:0000256|HAMAP-Rule:MF_01252}.
CC -!- SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins
CC subfamily. {ECO:0000256|ARBA:ARBA00008414, ECO:0000256|HAMAP-
CC Rule:MF_01252}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family.
CC {ECO:0000256|ARBA:ARBA00006401, ECO:0000256|HAMAP-Rule:MF_01252}.
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DR EMBL; CP010028; AIZ45100.1; -; Genomic_DNA.
DR RefSeq; WP_039683756.1; NZ_CP010028.1.
DR AlphaFoldDB; A0A0A7KG75; -.
DR STRING; 1182571.QR90_08200; -.
DR KEGG; dsw:QR90_08200; -.
DR HOGENOM; CLU_003827_12_0_0; -.
DR Proteomes; UP000030634; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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-UniRule.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051409; P:response to nitrosative stress; IEA:InterPro.
DR CDD; cd08922; FHb-globin; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR Gene3D; 1.10.490.10; Globins; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_01252; Hmp; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43396; FLAVOHEMOPROTEIN; 1.
DR PANTHER; PTHR43396:SF3; FLAVOHEMOPROTEIN; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF46458; Globin-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|HAMAP-Rule:MF_01252};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01252};
KW Heme {ECO:0000256|HAMAP-Rule:MF_01252, ECO:0000256|RuleBase:RU000356};
KW Iron {ECO:0000256|HAMAP-Rule:MF_01252};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01252};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01252};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01252};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01252};
KW Oxygen transport {ECO:0000256|HAMAP-Rule:MF_01252,
KW ECO:0000256|RuleBase:RU000356};
KW Reference proteome {ECO:0000313|Proteomes:UP000030634};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01252, ECO:0000256|RuleBase:RU000356}.
FT DOMAIN 5..134
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 152..266
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 149..412
FT /note="Reductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01252"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT BINDING 206..209
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT BINDING 278..283
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT BINDING 399..402
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT SITE 29
FT /note="Involved in heme-bound ligand stabilization and O-O
FT bond activation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT SITE 84
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT SITE 398
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
SQ SEQUENCE 412 AA; 44630 MW; 5D21D26D6538316D CRC64;
MLTPDQLSVV KATVPALEAH GETITRHFYA SMFAAHPELL NIFNPANQKT GKQARSLAAS
VLAYAANIDH PERLGGMVGR IAHKHVSLEV LPEHYPIVGE HLLGAIATVL GDAATPEILD
AWAAAYGQLA DIMIGVERGM YAGAAQQPGG WPGFKPFRVV KKVQESRVIA SLVLAPVDGQ
PLPPFQPGQY LSLQVRVPGG ETTQIRQYSL SDAPNGQTYR ISVKRELAPE HDPFAPGGLI
SNHLHDDVGV GDELLVHTPA GDFALQDSDR PVVLLSGGVG ITPMLSMLHA LAAGNSERPV
LFVHAALGRW HHAFRDQVNA LAQAHPNIRK VVYYTDVTDE DLAGEHHDET GLIRLETLRP
YLPAGEAEFY YCGPEGFTRA VEGILDRLHV PAERRFTETF GPSQDFVPVL TA
//
