ID A0A0T9SWM9_YERAL Unreviewed; 396 AA. AC A0A0T9SWM9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 10-OCT-2018, entry version 18. 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) CC and NAD(P)H to convert NO to nitrate, which protects the bacterium CC from various noxious nitrogen compounds. Therefore, plays a CC central role in the inducible response to nitrosative stress. CC {ECO:0000256|HAMAP-Rule:MF_01252}. CC -!- CATALYTIC ACTIVITY: 2 nitric oxide + 2 O(2) + NAD(P)H = 2 nitrate CC + NAD(P)(+) + H(+). {ECO:0000256|HAMAP-Rule:MF_01252}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP- CC 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01252}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per CC subunit. {ECO:0000256|HAMAP-Rule:MF_01252}; CC -!- DOMAIN: Consists of two distinct domains; an N-terminal heme- CC containing oxygen-binding domain and a C-terminal reductase domain CC with binding sites for FAD and NAD(P)H. {ECO:0000256|HAMAP- CC Rule:MF_01252}. CC -!- SIMILARITY: Belongs to the globin family. Two-domain CC flavohemoproteins subfamily. {ECO:0000256|HAMAP-Rule:MF_01252}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. CC {ECO:0000256|HAMAP-Rule:MF_01252}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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_CQEJ01000001.1. DR EnsemblBacteria; CNK43868; CNK43868; ERS137965_00059. 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; IPR001221; Phe_hydroxylase. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. 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; 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 Complete proteome {ECO:0000313|Proteomes:UP000041595}; KW Detoxification {ECO:0000256|HAMAP-Rule:MF_01252}; KW Dioxygenase {ECO:0000313|EMBL:CNK43868.1}; KW FAD {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 ECO:0000256|SAAS:SAAS01058403}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01252}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01252}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01252, KW ECO:0000256|SAAS:SAAS01058373, 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, KW ECO:0000256|RuleBase:RU000356}. FT DOMAIN 1 136 GLOBIN. {ECO:0000259|PROSITE:PS01033}. FT DOMAIN 150 255 FAD-binding FR-type. FT {ECO:0000259|PROSITE:PS51384}. FT NP_BIND 204 207 FAD. {ECO:0000256|HAMAP-Rule:MF_01252}. FT NP_BIND 268 273 NADP. {ECO:0000256|HAMAP-Rule:MF_01252}. FT NP_BIND 389 392 FAD. {ECO:0000256|HAMAP-Rule:MF_01252}. FT REGION 147 396 Reductase. {ECO:0000256|HAMAP-Rule: FT MF_01252}. FT REGION 259 396 NAD or NADP-binding. {ECO:0000256|HAMAP- FT Rule:MF_01252}. FT ACT_SITE 95 95 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_01252}. FT ACT_SITE 135 135 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_01252}. FT METAL 85 85 Iron (heme proximal ligand). FT {ECO:0000256|HAMAP-Rule:MF_01252}. FT BINDING 188 188 FAD. {ECO:0000256|HAMAP-Rule:MF_01252}. FT SITE 29 29 Involved in heme-bound ligand FT stabilization and O-O bond activation. FT {ECO:0000256|HAMAP-Rule:MF_01252}. FT SITE 84 84 Influences the redox potential of the FT prosthetic heme and FAD groups. FT {ECO:0000256|HAMAP-Rule:MF_01252}. FT SITE 388 388 Influences the redox potential of the FT prosthetic heme and FAD groups. FT {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 //