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HMP_BURST
ID   HMP_BURST               Reviewed;         393 AA.
AC   Q8GAZ4;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Flavohemoprotein {ECO:0000255|HAMAP-Rule:MF_01252};
DE   AltName: Full=Flavohemoglobin {ECO:0000255|HAMAP-Rule:MF_01252};
DE   AltName: Full=Hemoglobin-like protein {ECO:0000255|HAMAP-Rule:MF_01252};
DE   AltName: Full=Nitric oxide dioxygenase {ECO:0000255|HAMAP-Rule:MF_01252};
DE            Short=NO oxygenase {ECO:0000255|HAMAP-Rule:MF_01252};
DE            Short=NOD {ECO:0000255|HAMAP-Rule:MF_01252};
DE            EC=1.14.12.17 {ECO:0000255|HAMAP-Rule:MF_01252};
GN   Name=hmp {ECO:0000255|HAMAP-Rule:MF_01252};
OS   Burkholderia sp. (strain TH2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=109791;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12270830; DOI=10.1128/jb.184.20.5714-5722.2002;
RA   Suzuki K., Ichimura A., Ogawa N., Hasebe A., Miyashita K.;
RT   "Differential expression of two catechol 1,2-dioxygenases in Burkholderia
RT   sp. strain TH2.";
RL   J. Bacteriol. 184:5714-5722(2002).
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:0000255|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; Evidence={ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01252};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01252};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01252};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01252};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|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.
CC   -!- SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01252}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01252}.
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DR   EMBL; AB035325; BAC16771.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GAZ4; -.
DR   SMR; Q8GAZ4; -.
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; IPR000951; Ph_dOase_redase.
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; PR00409; PHDIOXRDTASE.
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; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP;
KW   Oxidoreductase; Oxygen transport; Transport.
FT   CHAIN           1..393
FT                   /note="Flavohemoprotein"
FT                   /id="PRO_0000052428"
FT   DOMAIN          153..256
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   REGION          1..139
FT                   /note="Globin"
FT   REGION          150..393
FT                   /note="Reductase"
FT   ACT_SITE        95
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         191
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         205..208
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         268..273
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         385..388
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   SITE            29
FT                   /note="Involved in heme-bound ligand stabilization and O-O
FT                   bond activation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   SITE            84
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   SITE            384
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
SQ   SEQUENCE   393 AA;  43707 MW;  D17DB36399BB717B CRC64;
     MLSAEHRAIV KATVPLLESG GEALTTHFYK TMLAEYPSVR PLFNQAHQQS GDQPRALANA
     VLMYARHIDQ LEQLGGLVSQ IVNKHVALNI LPEHYPIVGA CLLRAIREVL GAEIATDAVI
     EAWGAAYQQL ADLLIGLEEN VYVEKETATG GWRGTRAFVV ARKVKESDEI TSFYLRPADG
     GELLEFHPGQ YIGLKLIVDG EEIRRNYSLS AAANGREYRI SVKREPNGKA SNYLHDSVNE
     GATLDLLTPS GDFTLEHNDK PLVLISGGVG ITPTLAMLNA ALQTSRPIHF IHATRHGGVH
     AFRDHIDELA ARHPQLKRFY VYEKPRHDDE AHHAEGYIDE ARLIEWLPAT RDVDVYFLGP
     KSFMQAVKRH LKTIGVPEKQ SRYEFFGPAS ALD
 
 
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