ID E1J3N7_ECOLX Unreviewed; 403 AA.
AC E1J3N7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 ECO:0000313|EMBL:EFK69610.1};
GN ORFNames=HMPREF9347_01495 {ECO:0000313|EMBL:EFK69610.1};
OS Escherichia coli MS 124-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679205 {ECO:0000313|EMBL:EFK69610.1, ECO:0000313|Proteomes:UP000003390};
RN [1] {ECO:0000313|EMBL:EFK69610.1, ECO:0000313|Proteomes:UP000003390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 124-1 {ECO:0000313|EMBL:EFK69610.1,
RC ECO:0000313|Proteomes:UP000003390};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2010) 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: 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:EFK69610.1}.
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DR EMBL; ADWT01000008; EFK69610.1; -; Genomic_DNA.
DR AlphaFoldDB; E1J3N7; -.
DR Proteomes; UP000003390; 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 CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR CDD; cd14776; HmpEc-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|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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01252};
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 7..141
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 157..262
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 154..403
FT /note="Reductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT ACT_SITE 102
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT BINDING 92
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 195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT BINDING 211..214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT BINDING 275..280
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT BINDING 396..399
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT SITE 36
FT /note="Involved in heme-bound ligand stabilization and O-O
FT bond activation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT SITE 91
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT SITE 395
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
SQ SEQUENCE 403 AA; 44750 MW; 0A8FB37D71EC507F CRC64;
MQKKEDHMLD AQTIATVKAT IPLLVETGPK LTAHFYDRMF THNPELKEIF NMSNQRNGDQ
REALFNAIAA YASNIENLPA LLPAVEKIAQ KHTSFQIKPE QYNIVGEHLL ATLDEMFSPG
QEVLDAWGKA YGVLANVFIN REAEIYNENA SKAGGWEGTR DFRIVAKTPR SALITSFELE
PVDGGAVAEY RPGQYLGVWL KPEGFPHQEI RQYSLTRKPD GKGYRIAVKR EEGGQVSNWL
HNHANVGDVV KLVAPAGDFF MAVADDTPVT LISAGVGQTP MLAMLDTLAK AGHTAQVNWF
HAAENGDVHA FADEVKELGQ SLPRFTAHTW YRQPSEADRA KGQFDSEGLM DLSKQEGAFS
DPTMQFYLCG PVGFMQFAAK QLVDLGVKQE NIHYECFGPH KVL
//
