ID A0A0T9SWM9_YERAL Unreviewed; 396 AA. AC A0A0T9SWM9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 29-SEP-2021, entry version 26. 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=fsrB {ECO:0000313|EMBL:CNK43868.1}; GN Synonyms=hmp {ECO:0000256|HAMAP-Rule:MF_01252}; GN ORFNames=ERS137965_00059 {ECO:0000313|EMBL:CNK43868.1}; OS Yersinia aldovae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=29483 {ECO:0000313|EMBL:CNK43868.1, ECO:0000313|Proteomes:UP000041595}; RN [1] {ECO:0000313|EMBL:CNK43868.1, ECO:0000313|Proteomes:UP000041595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP06005 {ECO:0000313|EMBL:CNK43868.1, RC ECO:0000313|Proteomes:UP000041595}; RA Murphy D.; RL Submitted (MAR-2015) 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: 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; CQEJ01000001; CNK43868.1; -; Genomic_DNA. DR RefSeq; WP_042839644.1; NZ_CABHPY010000063.1. DR STRING; 527002.yaldo0001_23880; -. DR EnsemblBacteria; CNK43868; CNK43868; ERS137965_00059. DR eggNOG; COG1017; Bacteria. DR eggNOG; COG1018; Bacteria. DR Proteomes; UP000041595; 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 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; 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:SF3; PTHR43396:SF3; 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 SUPFAM; SSF46458; SSF46458; 1. DR SUPFAM; SSF52343; SSF52343; 1. DR SUPFAM; SSF63380; SSF63380; 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}; Dioxygenase {ECO:0000313|EMBL:CNK43868.1}; 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:CNK43868.1}; 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..136 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 NP_BIND 204..207 FT /note="FAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" FT NP_BIND 268..273 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" FT NP_BIND 389..392 FT /note="FAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" FT REGION 147..396 FT /note="Reductase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" FT REGION 259..396 FT /note="NAD or NADP-binding" 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 METAL 85 FT /note="Iron (heme proximal ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252" FT BINDING 188 FT /note="FAD" 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; 44388 MW; BC7D88A22F4910F6 CRC64; MLDSQTIAIV KSTIPVLAAT GPKLTAHFYD RMFKHNPELK HIFNMSNQFN GDQREALFNA ICAYAANIDN LAALLPAVER IANKHASLNI QPEHYPIVGH HLISTLDELL SPGQEVLDAW GKAYGVLADV FIQREKQIYQ QSESATGGWR NLRRFRIIKK EMQSEVICSF VLAPEDGGRV LDFKPGQYLG IYIEDESLEY QEIRQYSLTA APNGKTYRIA VKREEQGTVS NYLHGKLNEG DSVRIAPPRG DFFLDVSPQT PVALISAGVG QTPMLSMLNT LHSQQHAAPV HWLHAAENGR VHAFADEIAA IAENMPNLSR HVWYREPTAQ DGQGEDYHSK GFMDLSSHQW LAADPNRHYY FCGPVAFMQF AGRQLLAQGV AAERIHYECF GPHKVI //