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HAMAP rule MF_01252

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General rule information [?]

Accession MF_01252
Dates 24-AUG-2004 (Created)
26-JAN-2023 (Last updated, Version 34)
Name Hmp
Scope(s) Bacteria
Template(s) P24232 (HMP_ECOLI); P39662 (HMP_CUPNH); P26353 (HMP_SALTY); [ Recover all ]
Triggered by HAMAP; MF_01252 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier HMP
Protein name RecName: Full=Flavohemoprotein;
AltName: Full=Flavohemoglobin;
AltName: Full=Hemoglobin-like protein;
AltName: Full=Nitric oxide dioxygenase;
                 Short=NO oxygenase;
                 Short=NOD;
                 EC=1.14.12.17;
Gene name Name=hmp;

Comments [?]

case <OC:Pseudomonadota> or <OC:Bacillales>
FUNCTIONIs involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
end case
CATALYTIC ACTIVITY Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate; Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.12.17;
CATALYTIC ACTIVITY Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate; Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.17;
COFACTOR Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
COFACTOR Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.;
DOMAINConsists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
SIMILARITYBelongs to the globin family. Two-domain flavohemoproteins subfamily.
SIMILARITYIn the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Keywords [?]

case <OC:Pseudomonadota> or <OC:Bacillales>
Detoxification
end case
FAD
Flavoprotein
Heme
Iron
Metal-binding
NAD
NADP
Oxidoreductase
Oxygen transport
Transport

Gene Ontology [?]

GO:0005344; Molecular function:oxygen carrier activity
GO:0008941; Molecular function:nitric oxide dioxygenase activity
GO:0015671; Biological process:oxygen transport

Cross-references [?]

Pfam PF00970; FAD_binding_6; 1;
Pfam PF00042; Globin; 1;
Pfam PF00175; NAD_binding_1; 1;
PRINTS PR00371; FPNCR; 1;
PRINTS PR00410; PHEHYDRXLASE; 1;
PRINTS PR00188; PLANTGLOBIN; 1;
PRINTS PR00406; CYTB5RDTASE; 1;
PRINTS PR00409; PHDIOXRDTASE; 1;
PROSITE PS01033; GLOBIN; 1;
PROSITE PS51384; FAD_FR; 1;

Features [?]

From: HMP_ECOLI (P24232)
Key From To Description Tag Condition FTGroup
DOMAIN 151 251 /note="FAD-binding"
BINDING 204 207 /ligand="FAD"
/ligand_id="ChEBI:CHEBI:57692"
R-[QN]-Y-S
BINDING 268 273 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"
G-[VI]-G-[QILAV]-T-P
BINDING 389 392 /ligand="FAD"
/ligand_id="ChEBI:CHEBI:57692"
[CLFVT]-F-G-[PST]
REGION 147 Cter /note="Reductase"
ACT_SITE 95 95 /note="Charge relay system" Y
ACT_SITE 135 135 /note="Charge relay system" E
BINDING 85 85 /ligand="heme b"
/ligand_id="ChEBI:CHEBI:60344"
/ligand_part="Fe"
/ligand_part_id="ChEBI:CHEBI:18248"
/note="proximal binding residue"
H
BINDING 188 188 /ligand="FAD"
/ligand_id="ChEBI:CHEBI:57692"
Y
SITE 29 29 /note="Involved in heme-bound ligand stabilization and O-O bond activation" Y
SITE 84 84 /note="Influences the redox potential of the prosthetic heme and FAD groups" K
SITE 388 388 /note="Influences the redox potential of the prosthetic heme and FAD groups" E

Additional information [?]

Size range 392-411 amino acids
Related rules None
Fusion Nter: None Cter: None



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