HMP_RHOBA
ID HMP_RHOBA Reviewed; 408 AA.
AC Q7UIY1;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 104.
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}; Synonyms=fhp;
GN OrderedLocusNames=RB12262;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD77481.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294154; CAD77481.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_870404.1; NC_005027.1.
DR AlphaFoldDB; Q7UIY1; -.
DR SMR; Q7UIY1; -.
DR STRING; 243090.RB12262; -.
DR EnsemblBacteria; CAD77481; CAD77481; RB12262.
DR KEGG; rba:RB12262; -.
DR PATRIC; fig|243090.15.peg.5920; -.
DR eggNOG; COG1017; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_12_0_0; -.
DR InParanoid; Q7UIY1; -.
DR OrthoDB; 1834577at2; -.
DR Proteomes; UP000001025; Chromosome.
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; 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:SF3; PTHR43396:SF3; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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..408
FT /note="Flavohemoprotein"
FT /id="PRO_0000052443"
FT DOMAIN 152..263
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT REGION 1..138
FT /note="Globin"
FT REGION 149..408
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 205..208
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT BINDING 277..282
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT BINDING 398..401
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 397
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
SQ SEQUENCE 408 AA; 44911 MW; B33B7EBC66316C1C CRC64;
MLSEKTIRIV KEITPLVAAN AETITRRFYE RMFEANPEVK AFFNQAHQHS GGQQKALAGA
ICAYFTHIDN PAVLMPAVEL IAQKHVSLGI KPEHYPIVGS NLLAAIGDVM GDAATPEIVE
AVSEAYGFLA DIFIGREGAI YEEQASMPGG WNGTRTFVVT KKVRESEIVT SFYLKPEDEG
PLPPFKPGQY ITVHMDHPHT PTSPRNYSLS DCASQPHYRI SVKREERLVP DAPDGLISNH
LHDGIEEGHR IELGPPCGEF TVDPATIAKP IVLIAGGIGV TPLLSMAKSI VHANPNAELH
FIQAARNSKV HAFADELRRL AQAGPNVHTK VIYDSPLPGD VEEGKCDEAG FVTENQIRES
TPFTDADFYF CGPKPFMKNV HSCLRELGVD EHRVRYEFFG PKEELVAV
