ID   HMP_HALH5               Reviewed;         411 AA.
AC   Q9RC40;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 137.
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=BH1058;
OS   Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Halalkalibacterium (ex Joshi et al. 2022).
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=10484179; DOI=10.1007/s007920050120;
RA   Takami H., Takaki Y., Nakasone K., Sakiyama T., Maeno G., Sasaki R.,
RA   Hirama C., Fuji F., Masui N.;
RT   "Genetic analysis of the chromosome of alkaliphilic Bacillus halodurans C-
RT   125.";
RL   Extremophiles 3:227-233(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01252}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 nitric oxide + NADPH + 2 O2 = 2 nitrate + NADP(+) + H(+);
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=2 nitric oxide + NADH + 2 O2 = 2 nitrate + NAD(+) + H(+);
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; Evidence={ECO:0000255|HAMAP-
CC         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; Evidence={ECO:0000255|HAMAP-
CC         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; AB024563; BAA83959.1; -; Genomic_DNA.
DR   EMBL; BA000004; BAB04777.1; -; Genomic_DNA.
DR   PIR; B83782; B83782.
DR   RefSeq; WP_010897228.1; NC_002570.2.
DR   AlphaFoldDB; Q9RC40; -.
DR   SMR; Q9RC40; -.
DR   STRING; 272558.gene:10726952; -.
DR   KEGG; bha:BH1058; -.
DR   eggNOG; COG1017; Bacteria.
DR   eggNOG; COG1018; Bacteria.
DR   HOGENOM; CLU_003827_12_0_9; -.
DR   OrthoDB; 9801223at2; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0008941; F:nitric oxide dioxygenase [NAD(P)H] 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:0071500; P:cellular response to nitrosative stress; IEA:TreeGrafter.
DR   GO; GO:0046210; P:nitric oxide catabolic process; IEA:TreeGrafter.
DR   CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR   CDD; cd14777; Yhb1-globin-like; 1.
DR   FunFam; 1.10.490.10:FF:000003; Flavohemoprotein; 1.
DR   FunFam; 2.40.30.10:FF:000034; Flavohemoprotein; 1.
DR   FunFam; 3.40.50.80:FF:000010; Flavohemoprotein; 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; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR   NCBIfam; NF009805; PRK13289.1; 1.
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   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
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   Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP;
KW   Oxidoreductase; Oxygen transport; Reference proteome; Transport.
FT   CHAIN           1..411
FT                   /note="Flavohemoprotein"
FT                   /id="PRO_0000052422"
FT   DOMAIN          5..142
FT                   /note="Globin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   DOMAIN          156..267
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   REGION          153..411
FT                   /note="Reductase"
FT   ACT_SITE        99
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   ACT_SITE        141
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         89
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         194
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         210..213
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         280..285
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         401..404
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   SITE            33
FT                   /note="Involved in heme-bound ligand stabilization and O-O
FT                   bond activation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   SITE            88
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   SITE            400
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
SQ   SEQUENCE   411 AA;  46565 MW;  779B2F4AB64EA5DE CRC64;
     MSTATLSQET KQIVKATVPI LAEHGEAITK HFYKRMFSHH PELLNIFNQT HQKQGRQPQA
     LANSIYAAAE HIDNLEAILP VVSRIAHKHR SLNIKPEQYP IVGENLLAAM REVLGDAASD
     DVLEAWREAY ELIADVFIQV EKKMYEEASQ APGGWREFRS FVVEKKQRES ATITSFYLKP
     EDGKALASYK PGQYITVKVT IPGHEHTHMR QYSLSDAPEK GYYRITVKRE EGDGDLPPGI
     VSNYLHQHIH EGDVLEITAP AGDFTLQEEG ERPIVFISGG VGITPLMSMF NTLMQRGVKR
     EVIFIHAAIN GFYHAMHDHL AQTASQQENV HYAVCYERPT PGDRMNPFMK KEGFIDESFL
     RSILHDREAD FYFCGPVPFM KTIAQILKDW DVPEQQVHYE FFGPAGTLAS S
//