AC   MF_01252;
DC   Protein; auto
TR   HAMAP; MF_01252; -; 1; level=0
XX
Names: Hmp
XX
ID   HMP
DE   RecName: Full=Flavohemoprotein;
DE   AltName: Full=Flavohemoglobin;
DE   AltName: Full=Hemoglobin-like protein;
DE   AltName: Full=Nitric oxide dioxygenase;
DE            Short=NO oxygenase;
DE            Short=NOD;
DE            EC=1.14.12.17;
GN   Name=hmp;
XX
case <OC:Pseudomonadota> or <OC:Bacillales>
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 bacterium from
CC       various noxious nitrogen compounds. Therefore, plays a central role in
CC       the inducible response to nitrosative stress.
end case
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=heme b; Xref=ChEBI:CHEBI:60344;
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per subunit.;
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.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
XX
DR   Pfam; PF00970; FAD_binding_6; 1; trigger=no
DR   Pfam; PF00042; Globin; 1; trigger=no
DR   Pfam; PF00175; NAD_binding_1; 1; trigger=no
DR   PRINTS; PR00371; FPNCR; 1; trigger=no
DR   PRINTS; PR00410; PHEHYDRXLASE; 1; trigger=no
DR   PRINTS; PR00188; PLANTGLOBIN; 1; trigger=no
DR   PRINTS; PR00406; CYTB5RDTASE; 1; trigger=no
DR   PRINTS; PR00409; PHDIOXRDTASE; 1; trigger=no
DR   PROSITE; PS01033; GLOBIN; 1; trigger=yes
DR   PROSITE; PS51384; FAD_FR; 1; trigger=yes
XX
case <OC:Pseudomonadota> or <OC:Bacillales>
KW   Detoxification
end case
KW   FAD
KW   Flavoprotein
KW   Heme
KW   Iron
KW   Metal-binding
KW   NAD
KW   NADP
KW   Oxidoreductase
KW   Oxygen transport
KW   Transport
XX
GO   GO:0005344; F:oxygen carrier activity
GO   GO:0008941; F:nitric oxide dioxygenase activity
GO   GO:0015671; P:oxygen transport
XX
FT   From: HMP_ECOLI (P24232)
FT   BINDING         204..207
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: R-[QN]-Y-S
FT   BINDING         268..273
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: G-[VI]-G-[QILAV]-T-P
FT   BINDING         389..392
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: [CLFVT]-F-G-[PST]
FT   REGION          147..Cter
FT                   /note="Reductase"
FT   ACT_SITE        95
FT                   /note="Charge relay system"
FT   Condition: Y
FT   ACT_SITE        135
FT                   /note="Charge relay system"
FT   Condition: E
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   Condition: H
FT   BINDING         188
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: Y
FT   SITE            29
FT                   /note="Involved in heme-bound ligand stabilization and O-O
FT                   bond activation"
FT   Condition: Y
FT   SITE            84
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT   Condition: K
FT   SITE            388
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT   Condition: E
XX
Size: 392-411;
Related: None;
Template: P24232; P39662; P26353;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in RALEU, RHIME
Comments: None
XX
# Revision 1.35 2024/01/15
//