ID A0A9W3P2D0_BACTU Unreviewed; 402 AA. AC A0A9W3P2D0; DT 08-NOV-2023, integrated into UniProtKB/TrEMBL. DT 08-NOV-2023, sequence version 1. DT 24-JAN-2024, entry version 2. 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=BTF1_04945 {ECO:0000313|EMBL:AFQ25210.1}; OS Bacillus thuringiensis HD-789. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1217737 {ECO:0000313|EMBL:AFQ25210.1, ECO:0000313|Proteomes:UP000005257}; RN [1] {ECO:0000313|EMBL:AFQ25210.1, ECO:0000313|Proteomes:UP000005257} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HD-789 {ECO:0000313|EMBL:AFQ25210.1, RC ECO:0000313|Proteomes:UP000005257}; RX PubMed=24309743; RA Doggett N.A., Stubben C.J., Chertkov O., Bruce D.C., Detter J.C., RA Johnson S.L., Han C.S.; RT "Complete Genome Sequence of Bacillus thuringiensis Serovar Israelensis RT Strain HD-789."; RL Genome Announc. 1:e01023-e01013(2013). 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00238}. 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; CP003763; AFQ25210.1; -; Genomic_DNA. DR RefSeq; WP_000947319.1; NC_018508.1. DR Proteomes; UP000005257; Chromosome. DR GO; GO:0051213; F:dioxygenase activity; 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; 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|HAMAP-Rule:MF_01252}; KW Dioxygenase {ECO:0000313|EMBL:AFQ25210.1}; KW FAD {ECO:0000256|HAMAP-Rule:MF_01252}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW 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|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01252}; KW Oxygen transport {ECO:0000256|ARBA:ARBA00022621, ECO:0000256|HAMAP- KW Rule:MF_01252}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01252}. FT DOMAIN 1..133 FT /note="Globin family profile" FT /evidence="ECO:0000259|PROSITE:PS01033" FT DOMAIN 150..260 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000259|PROSITE:PS51384" FT REGION 147..402 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 135 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 188 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" FT BINDING 204..207 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" FT BINDING 273..278 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" FT BINDING 394..397 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 393 FT /note="Influences the redox potential of the prosthetic FT heme and FAD groups" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" SQ SEQUENCE 402 AA; 45004 MW; 144AB70C9845008B CRC64; MLSAKTIEIV KSTVPLLQEK GVEITTRFYE ILFSEHPELL NIFNHTNQKK GRQQQALANA VYAAATYIDN LEAIIPVVKQ IGHKHRSLGI KAEHYPIVGT CLLRAIKEVA GAPDEVLNAW GEAYGVIADA FISIEAEMYE EAAHKEGGWK DFRNFVIVKK VKESDVITSF YLKPEDGGKV SSFIPGQYVT VQINIEGETY THNRQYSLSD APGKEYYRIS VKKEKGVDTP DGKVSNYLHE HVKEGDVLPV SAPAGDFVLN MDSTLPVVLI SGGVGITPMM SMLNTLIEQD SKRNVYFIHA AINSNTHAMK EHVKAVENEY EQVKAYTCYS APTEKDLEMK NFDKEGFVES EWLKTIIQTT EAEFYFCGPV AFMKHINAAL TDLGVKQEHI HYEFFGPATS LQ //