ID A0A418X8W0_9PSED Unreviewed; 403 AA.
AC A0A418X8W0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=D3879_24070 {ECO:0000313|EMBL:RJG08925.1};
OS Pseudomonas cavernicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2320866 {ECO:0000313|EMBL:RJG08925.1, ECO:0000313|Proteomes:UP000284021};
RN [1] {ECO:0000313|EMBL:RJG08925.1, ECO:0000313|Proteomes:UP000284021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1S02-6 {ECO:0000313|EMBL:RJG08925.1,
RC ECO:0000313|Proteomes:UP000284021};
RA Zhu H.;
RL Submitted (SEP-2018) 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.
CC {ECO:0000256|ARBA:ARBA00025094, ECO:0000256|HAMAP-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:RJG08925.1}.
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DR EMBL; QYUR01000008; RJG08925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418X8W0; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000284021; 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; cd14779; FHP_Ae-globin-like; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 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 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; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
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|ARBA:ARBA00022575, ECO:0000256|HAMAP-
KW Rule:MF_01252};
KW FAD {ECO:0000256|ARBA:ARBA00022827, 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 ECO:0000313|EMBL:RJG08925.1};
KW Oxygen transport {ECO:0000256|HAMAP-Rule:MF_01252,
KW ECO:0000256|RuleBase:RU000356};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01252, ECO:0000256|RuleBase:RU000356}.
FT DOMAIN 9..134
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 152..262
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 149..403
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 275..280
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT BINDING 395..398
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 394
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
SQ SEQUENCE 403 AA; 44657 MW; 0745CD04F01A7CB4 CRC64;
MLTQKTKDIV KATAPVLAEH GYGIIKCFYK RMFEAHPELK NVFNMAHQEQ GQQQQALARA
VYAYAENIED PSSLMAVLKN IANKHASLGV KPEQYPIVGE HLLAAIKEVL GDAATDDIIS
AWAQAYGNLA DVLIGMESEL YERSAEQPGG WKGWRSFVVR EKRPESDVIT SFILAPVDGG
PVVNFEPGQY TSVAIDVPTL GLQQIRQYSL SDMPNGRSYR ISVKREGGGT QPPGYVSNLL
HDHVNVGDEV KLAAPYGSFH IDVNAKTPLV LISGGVGLTP MVSMLKAALQ APPRHVVFVH
GARNSAVHAM RDRLREAAKS YENFDLFVFY DQPLPEDVQG RDYDYPGLVD VKQIEKSILL
PDADYYICGP IPFMRMQHDA LKNLGIHEAR IHYEVFGPDL FAE
//
