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HMP_SHIFL
ID   HMP_SHIFL               Reviewed;         396 AA.
AC   Q7C0F9; Q83QJ4;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=hmpA;
GN   OrderedLocusNames=SF2599, S2771;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(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; AE005674; AAN44096.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17920.1; -; Genomic_DNA.
DR   RefSeq; NP_708389.1; NC_004337.2.
DR   RefSeq; WP_000883129.1; NZ_WPGW01000021.1.
DR   AlphaFoldDB; Q7C0F9; -.
DR   SMR; Q7C0F9; -.
DR   STRING; 198214.SF2599; -.
DR   EnsemblBacteria; AAN44096; AAN44096; SF2599.
DR   EnsemblBacteria; AAP17920; AAP17920; S2771.
DR   GeneID; 1026953; -.
DR   GeneID; 58390598; -.
DR   KEGG; sfl:SF2599; -.
DR   KEGG; sfx:S2771; -.
DR   PATRIC; fig|198214.7.peg.3104; -.
DR   HOGENOM; CLU_003827_12_0_6; -.
DR   OMA; ADIHYEV; -.
DR   OrthoDB; 1834577at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome; Transport.
FT   CHAIN           1..396
FT                   /note="Flavohemoprotein"
FT                   /id="PRO_0000052448"
FT   DOMAIN          150..255
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   REGION          1..136
FT                   /note="Globin"
FT   REGION          147..396
FT                   /note="Reductase"
FT   ACT_SITE        95
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   ACT_SITE        135
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         188
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT   BINDING         204..207
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         389..392
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            388
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
SQ   SEQUENCE   396 AA;  43912 MW;  0930DB697EF517C7 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 DFFMAVADDT PVTLISTGVG QTPMLAMLDT LAKAGHTAQV NWFHAAENGE
     VHAFADEVKE LGQSLPRFTA HTWYRQPSEA DRAKGQFDSE GLMDLSKLEG AFSDPTMQFY
     LCGPVGFMQF TAKQLVDLGV KQENIHYECF GPHKVL
 
 
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