ID HMP_VIBVY Reviewed; 394 AA. AC Q7MH09; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 02-SEP-2026, entry version 126. 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=VV3064; OS Vibrio vulnificus (strain YJ016). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=196600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJ016; RX PubMed=14656965; DOI=10.1101/gr.1295503; RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L., RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P., RA Lee C.-T., Hor L.-I., Tsai S.-F.; RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen."; RL Genome Res. 13:2577-2587(2003). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000037; BAC95828.1; -; Genomic_DNA. DR RefSeq; WP_011151324.1; NC_005139.1. DR AlphaFoldDB; Q7MH09; -. DR SMR; Q7MH09; -. DR STRING; 672.VV93_v1c27920; -. DR KEGG; vvy:VV3064; -. DR eggNOG; COG1017; Bacteria. DR eggNOG; COG1018; Bacteria. DR HOGENOM; CLU_003827_12_0_6; -. 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; cd14776; HmpEc-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; 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; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; KW Oxidoreductase; Oxygen transport; Transport. FT CHAIN 1..394 FT /note="Flavohemoprotein" FT /id="PRO_0000052452" FT DOMAIN 1..136 FT /note="Globin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238" FT DOMAIN 150..255 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252" FT REGION 147..394 FT /note="Reductase" FT ACT_SITE 95 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252" FT ACT_SITE 135 FT /note="Charge relay system" FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01252" FT BINDING 188 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252" FT BINDING 204..207 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252" FT BINDING 268..273 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252" FT BINDING 387..390 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252" FT SITE 29 FT /note="Involved in heme-bound ligand stabilization and O-O FT bond activation" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252" FT SITE 84 FT /note="Influences the redox potential of the prosthetic FT heme and FAD groups" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252" FT SITE 386 FT /note="Influences the redox potential of the prosthetic FT heme and FAD groups" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252" SQ SEQUENCE 394 AA; 44233 MW; 39FC408D27DE78D3 CRC64; MLSENTINIV KSTAPLLAET GPKLTAHFYQ RMFEHNPELK DIFNMSNQRN GDQREALFNA ICAYASNIDN LPALLGAVEK IAHKHSSFLI TADQYQIVGS HLLATIDELF SPGQAVLDAW AEAYGVLANV FIQREEQIYQ ANQSQTGGWR GLREFELVEK QYESAHICSF VFKPVDGGSV VSFKPGQYLG IYINDEQFEN QEIRQYSLSS SVRPDCYRIS VKREEGGRVS NYLHDHLDVG SKVKLAAPAG DFFLDAAPTA PVVLISAGVG LTPTLSMLES LTEHQAPVTW IHATENGQQH AFKQHVKQLV ETHPHFNSLV WYNQPNSDDK IGDDFQFSGW VNLHEIETVL KQADVQVYFC GPVGFMQFIA KQLLEMGVPE QQFHYECFGP HKVV //