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HMP_BORPA
ID   HMP_BORPA               Reviewed;         402 AA.
AC   Q7TTP2;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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}; Synonyms=fhp;
GN   OrderedLocusNames=BPP1637;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640428; CAE36938.1; -; Genomic_DNA.
DR   RefSeq; WP_003810868.1; NC_002928.3.
DR   AlphaFoldDB; Q7TTP2; -.
DR   SMR; Q7TTP2; -.
DR   EnsemblBacteria; CAE36938; CAE36938; BPP1637.
DR   KEGG; bpa:BPP1637; -.
DR   HOGENOM; CLU_003827_12_0_4; -.
DR   OMA; ADIHYEV; -.
DR   Proteomes; UP000001421; Chromosome.
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; 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   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..402
FT                   /note="Flavohemoprotein"
FT                   /id="PRO_0000052426"
FT   DOMAIN          152..261
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   REGION          1..138
FT                   /note="Globin"
FT   REGION          149..402
FT                   /note="Reductase"
FT   ACT_SITE        95
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   ACT_SITE        137
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         190
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         206..209
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         274..279
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         395..398
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            394
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
SQ   SEQUENCE   402 AA;  43723 MW;  0231E77F0A3C71E6 CRC64;
     MLSPEVRALV KATAPVLKEH GEALTRHFYT RMLGGNPELR QLFNQGHQQS GQQQQALAAA
     VAAYAEHIDD PSVLLPVVER IAHKHVSLGV RAEHYAIVGK HLLASIREVL GEAATDELID
     AWAAAYGQLA DLLIGRERAL YAAAASRDGG WTGWRAFKVV RKTPESAEIT SFYLAPADGG
     ATPDYLPGQY VSVRVYVPEL GLMQPRQYSL SEAPGMPGQL RISVKREAGS PAGMVSGTLH
     NRINEGDVLD VSPPQGDFTL DAEDGRPVVL LSGGVGLTPM VSMLNHLTAR DDGRQIRFVH
     ACREAGVHAM KEHINALAAK RPNVRKAVFY ERVGADDRRG VDYDYEGRVD LHAIRDEVIL
     PDADYYLCGP LPFMQAQRRA LADLGVAEHR IHAEVFGTGG VA
 
 
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