ID A0A1V4HNX8_9BACL Unreviewed; 404 AA.
AC A0A1V4HNX8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=BC351_21165 {ECO:0000313|EMBL:OPH59418.1};
OS Paenibacillus ferrarius.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1469647 {ECO:0000313|EMBL:OPH59418.1, ECO:0000313|Proteomes:UP000190626};
RN [1] {ECO:0000313|Proteomes:UP000190626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CY1 {ECO:0000313|Proteomes:UP000190626};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPH59418.1}.
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DR EMBL; MBTG01000007; OPH59418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4HNX8; -.
DR STRING; 1469647.BC351_21165; -.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000190626; Unassembled WGS sequence.
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 GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR CDD; cd14777; Yhb1-globin-like; 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 PRINTS; PR00406; CYTB5RDTASE.
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 {ECO:0000256|HAMAP-Rule:MF_01252};
KW Dioxygenase {ECO:0000313|EMBL:OPH59418.1};
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:UP000190626};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01252, ECO:0000256|RuleBase:RU000356}.
FT DOMAIN 1..134
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 152..263
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 149..404
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 276..281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT BINDING 397..400
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 396
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
SQ SEQUENCE 404 AA; 44774 MW; 2381DE5348AFB667 CRC64;
MLSQRTIEVI KSTVPVLEIH GTAITTRFYD MLFTAHPELL HIFNHANQKQ GKQQTALANA
VYAAALHIDR LEMILPVVKQ IAHKHRSLGV QAEHYPIVGK YLLAAIKDVL GDAASEDILQ
AWGEAYGVIA DAFIGIEADM YEQAKSQAGG WAGFRPFRII QKVKESDVIT SFYITPLDGG
ALAAFEPGQY ISVNVQIPGE EHAHIRQYSL SDASDKPYYR ISVKREDAIA DRPAGKVSVY
LHEQKEVGDI LPISAPAGDF TLDQQDSRPV VLISGGVGLT PMVSMLNTLA VTKPARQVTF
IHAARNGQLH AFKQQVETIA QQHSNLSIHW CYEKPNEQDL TEQAFHKQGY IDLNWLQTVV
PAKEACYYFC GPVPFMKAIN GDLLEWGIPA EDIHYEFFGP AGSL
//
