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Flavohemoprotein (Flavohemoglobin) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (EC 1.14.12.17)

 A0A0G3JHC6_ECOLX        Unreviewed;       396 AA.
A0A0G3JHC6;
16-SEP-2015, integrated into UniProtKB/TrEMBL.
16-SEP-2015, sequence version 1.
25-OCT-2017, entry version 15.
RecName: Full=Flavohemoprotein {ECO:0000256|HAMAP-Rule:MF_01252};
AltName: Full=Flavohemoglobin {ECO:0000256|HAMAP-Rule:MF_01252};
AltName: Full=Hemoglobin-like protein {ECO:0000256|HAMAP-Rule:MF_01252};
AltName: Full=Nitric oxide dioxygenase {ECO:0000256|HAMAP-Rule:MF_01252};
Short=NO oxygenase {ECO:0000256|HAMAP-Rule:MF_01252};
Short=NOD {ECO:0000256|HAMAP-Rule:MF_01252};
EC=1.14.12.17 {ECO:0000256|HAMAP-Rule:MF_01252};
Name=hmp {ECO:0000256|HAMAP-Rule:MF_01252};
ORFNames=APECO2_15425 {ECO:0000313|EMBL:AKK39979.1};
Escherichia coli APEC O2-211.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=1954351 {ECO:0000313|EMBL:AKK39979.1, ECO:0000313|Proteomes:UP000035478};
[1] {ECO:0000313|EMBL:AKK39979.1, ECO:0000313|Proteomes:UP000035478}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=APEC O2 {ECO:0000313|Proteomes:UP000035478};
Mangiamele P.M., Nicholson B.A., Nolan L.K.;
"Toolbox for Exploring Avian Pathogenic Escherichia coli (APEC)
Pathogenesis and Control.";
Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Is involved in NO detoxification in an aerobic process,
termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2)
and NAD(P)H to convert NO to nitrate, which protects the bacterium
from various noxious nitrogen compounds. Therefore, plays a
central role in the inducible response to nitrosative stress.
{ECO:0000256|HAMAP-Rule:MF_01252}.
-!- CATALYTIC ACTIVITY: 2 nitric oxide + 2 O(2) + NAD(P)H = 2 nitrate
+ NAD(P)(+) + H(+). {ECO:0000256|HAMAP-Rule:MF_01252}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000256|HAMAP-Rule:MF_01252};
Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01252};
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000256|HAMAP-Rule:MF_01252};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000256|HAMAP-Rule:MF_01252};
-!- DOMAIN: Consists of two distinct domains; an N-terminal heme-
containing oxygen-binding domain and a C-terminal reductase domain
with binding sites for FAD and NAD(P)H. {ECO:0000256|HAMAP-
Rule:MF_01252}.
-!- SIMILARITY: Belongs to the globin family. Two-domain
flavohemoproteins subfamily. {ECO:0000256|HAMAP-Rule:MF_01252}.
-!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
pyridine nucleotide cytochrome reductase family.
{ECO:0000256|HAMAP-Rule:MF_01252}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00238}.
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EMBL; CP006834; AKK39979.1; -; Genomic_DNA.
RefSeq; WP_000883131.1; NZ_CP006834.1.
Proteomes; UP000035478; Chromosome.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008941; F:nitric oxide dioxygenase activity; IEA:UniProtKB-UniRule.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-UniRule.
GO; GO:0051409; P:response to nitrosative stress; IEA:InterPro.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
HAMAP; MF_01252; Hmp; 1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like.
InterPro; IPR023950; Hmp.
InterPro; IPR008333; OxRdtase_FAD-bd_dom.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR001221; Phe_hydroxylase.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00970; FAD_binding_6; 1.
Pfam; PF00042; Globin; 1.
Pfam; PF00175; NAD_binding_1; 1.
PRINTS; PR00410; PHEHYDRXLASE.
SUPFAM; SSF46458; SSF46458; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS01033; GLOBIN; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000035478};
Detoxification {ECO:0000256|HAMAP-Rule:MF_01252};
Dioxygenase {ECO:0000313|EMBL:AKK39979.1};
FAD {ECO:0000256|HAMAP-Rule:MF_01252};
Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01252};
Heme {ECO:0000256|HAMAP-Rule:MF_01252, ECO:0000256|RuleBase:RU000356};
Iron {ECO:0000256|HAMAP-Rule:MF_01252, ECO:0000256|RuleBase:RU000356};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01252,
ECO:0000256|RuleBase:RU000356}; NAD {ECO:0000256|HAMAP-Rule:MF_01252};
NADP {ECO:0000256|HAMAP-Rule:MF_01252};
Oxidoreductase {ECO:0000313|EMBL:AKK39979.1};
Oxygen transport {ECO:0000256|HAMAP-Rule:MF_01252,
ECO:0000256|RuleBase:RU000356};
Transport {ECO:0000256|HAMAP-Rule:MF_01252,
ECO:0000256|RuleBase:RU000356}.
DOMAIN 1 134 GLOBIN. {ECO:0000259|PROSITE:PS01033}.
DOMAIN 150 255 FAD-binding FR-type.
{ECO:0000259|PROSITE:PS51384}.
NP_BIND 204 207 FAD. {ECO:0000256|HAMAP-Rule:MF_01252}.
NP_BIND 268 273 NADP. {ECO:0000256|HAMAP-Rule:MF_01252}.
NP_BIND 389 392 FAD. {ECO:0000256|HAMAP-Rule:MF_01252}.
REGION 147 396 Reductase. {ECO:0000256|HAMAP-
Rule:MF_01252}.
REGION 259 396 NAD or NADP-binding. {ECO:0000256|HAMAP-
Rule:MF_01252}.
ACT_SITE 95 95 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_01252}.
ACT_SITE 135 135 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_01252}.
METAL 85 85 Iron (heme proximal ligand).
{ECO:0000256|HAMAP-Rule:MF_01252}.
BINDING 188 188 FAD. {ECO:0000256|HAMAP-Rule:MF_01252}.
SITE 29 29 Involved in heme-bound ligand
stabilization and O-O bond activation.
{ECO:0000256|HAMAP-Rule:MF_01252}.
SITE 84 84 Influences the redox potential of the
prosthetic heme and FAD groups.
{ECO:0000256|HAMAP-Rule:MF_01252}.
SITE 388 388 Influences the redox potential of the
prosthetic heme and FAD groups.
{ECO:0000256|HAMAP-Rule:MF_01252}.
SEQUENCE 396 AA; 43863 MW; 1383EEF10A0CFC0A CRC64;
MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA
IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGE HLLATLDEMF SPGQEVLDAW
GKAYGVLANV FINREAEIYN ENASKAGGWE GTRDFRIVAK TPRSALITSF ELEPVDGGAV
AEYRPGQYLG VWLKPEGFPH QEIRQYSLTR KPDGKGYRIA VKREEGGQVS NWLHNHANVG
DVVKLVAPAG DFFMDVTDDT PVTLISAGVG QTPMLAMLDT LAKAGHTAQV NWLHAAENGD
VHAFADEVKE LGLSLPQFTA HTWYRQPSEA DRVKGQFDSE GLMDLSKLEG AFSDPTMQFY
LCGPVGFMQF AAKQLVDLGV KQENIHYECF GPHKVL


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