ID A0A5X8YPB6_SALET Unreviewed; 396 AA. AC A0A5X8YPB6; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 14-DEC-2022, entry version 14. 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=EVG56_08140 {ECO:0000313|EMBL:ECB1986405.1}; OS Salmonella enterica subsp. enterica serovar Kisarawe. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=2517242 {ECO:0000313|EMBL:ECB1986405.1}; RN [1] {ECO:0000313|EMBL:ECB1986405.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=508285 {ECO:0000313|EMBL:ECB1986405.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (JAN-2019) 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00238}. 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:ECB1986405.1}. 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; AAHWUP010000010; ECB1986405.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5X8YPB6; -. 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 Gene3D; 1.10.490.10; -; 1. DR Gene3D; 3.40.50.80; -; 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:SF3; FLAVOHEMOPROTEIN; 1. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00042; Globin; 1. DR Pfam; PF00175; NAD_binding_1; 1. 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:ECB1986405.1}; 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 1..134 FT /note="GLOBIN" FT /evidence="ECO:0000259|PROSITE:PS01033" FT DOMAIN 150..255 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000259|PROSITE:PS51384" FT REGION 147..396 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 268..273 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" FT BINDING 389..392 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 388 FT /note="Influences the redox potential of the prosthetic FT heme and FAD groups" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" SQ SEQUENCE 396 AA; 44004 MW; 9E2A5908F93FFEBF CRC64; MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGT HLLATLDEMF NPGQEVLDAW GKAYGVLANV FIHREAEIYH ENASKDGGWE GTRPFRIVAK TPRSALITSF EFEPVDGGTV AEYRPGQYLG VWLKPEGFAH QEIRQYSLTR KPDGKGYRIA VKREDGGQVS NWLHHHASVG DVVHLAAPAG DFFMNVAADT PVSLISAGVG QTPMLAMLDT LAKEQHTAQV NWFHAAENGD VHAFADEVSE LGRTLPRFTA HTWYREPTEA DRAQRVFDSE GLMDLSKLEA AISDPAMQFY LCGPVGFMQF AAKQLVSLGV NNENIHYECF GPHKVL //