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XDHD_ECOLI
ID   XDHD_ECOLI              Reviewed;         956 AA.
AC   Q46814; Q2M9V9;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Probable hypoxanthine oxidase XdhD;
DE            EC=1.-.-.-;
GN   Name=xdhD; Synonyms=ygfN; OrderedLocusNames=b2881, JW2849;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   FUNCTION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=10986234; DOI=10.1128/jb.182.19.5332-5341.2000;
RA   Xi H., Schneider B.L., Reitzer L.;
RT   "Purine catabolism in Escherichia coli and function of xanthine
RT   dehydrogenase in purine salvage.";
RL   J. Bacteriol. 182:5332-5341(2000).
CC   -!- FUNCTION: Probably has no xanthine dehydrogenase activity; however
CC       deletion results in increased adenine sensitivity, suggesting that this
CC       protein contributes to the conversion of adenine to guanine nucleotides
CC       during purine salvage. {ECO:0000269|PubMed:10986234}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC       Note=Binds 2 [2Fe-2S] centers. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U28375; AAA83062.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75919.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76947.1; -; Genomic_DNA.
DR   PIR; A65072; A65072.
DR   RefSeq; NP_417357.1; NC_000913.3.
DR   RefSeq; WP_000583615.1; NZ_LN832404.1.
DR   AlphaFoldDB; Q46814; -.
DR   SMR; Q46814; -.
DR   BioGRID; 4262328; 17.
DR   DIP; DIP-28056N; -.
DR   IntAct; Q46814; 3.
DR   STRING; 511145.b2881; -.
DR   PaxDb; Q46814; -.
DR   PRIDE; Q46814; -.
DR   EnsemblBacteria; AAC75919; AAC75919; b2881.
DR   EnsemblBacteria; BAE76947; BAE76947; BAE76947.
DR   GeneID; 949079; -.
DR   KEGG; ecj:JW2849; -.
DR   KEGG; eco:b2881; -.
DR   PATRIC; fig|1411691.4.peg.3853; -.
DR   EchoBASE; EB2876; -.
DR   eggNOG; COG1529; Bacteria.
DR   eggNOG; COG2080; Bacteria.
DR   HOGENOM; CLU_001681_2_3_6; -.
DR   InParanoid; Q46814; -.
DR   OMA; TSYIEWT; -.
DR   PhylomeDB; Q46814; -.
DR   BioCyc; EcoCyc:G7500-MON; -.
DR   BioCyc; MetaCyc:G7500-MON; -.
DR   PRO; PR:Q46814; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR   InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR017699; Mo-bd_YgfN/XdhD.
DR   PANTHER; PTHR11908; PTHR11908; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   PIRSF; PIRSF000127; Xanthine_DH; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF47741; SSF47741; 1.
DR   SUPFAM; SSF54665; SSF54665; 1.
DR   SUPFAM; SSF56003; SSF56003; 1.
DR   TIGRFAMs; TIGR03313; Se_sel_red_Mo; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW   Purine metabolism; Purine salvage; Reference proteome.
FT   CHAIN           1..956
FT                   /note="Probable hypoxanthine oxidase XdhD"
FT                   /id="PRO_0000166096"
FT   BINDING         414
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000255"
FT   BINDING         445
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000255"
FT   BINDING         727
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   956 AA;  103519 MW;  F60EEFE06F0AC17D CRC64;
     MIIHFTLNGA PQELTVNPGE NVQKLLFNMG MHSVRNSDDG FGFAGSDAII FNGNIVNASL
     LIAAQLEKAD IRTAESLGKW NELSLVQQAM VDVGVVQSGY NDPAAALIIT DLLDRIAAPT
     REEIDDALSG LFSRDAGWQQ YYQVIELAVA RKNNPQATID IAPTFRDDLE VIGKHYPKTD
     AAKMVQAKPC YVEDRVTADA CVIKMLRSPH AHALITHLDV SKAEALPGVV HVITHLNCPD
     IYYTPGGQSA PEPSPLDRRM FGKKMRHVGD RVAAVVAESE EIALEALKLI DVEYEVLKPV
     MSIDEAMAED APVVHDEPVV YVAGAPDTLE DDNSHAAQRG EHMIINFPIG SRPRKNIAAS
     IHGHIGDMDK GFADADVIIE RTYNSTQAQQ CPTETHICFT RMDGDRLVIH ASTQVPWHLR
     RQVARLVGMK QHKVHVIKER VGGGFGSKQD ILLEEVCAWA TCVTGRPVLF RYTREEEFIA
     NTSRHVAKVT VKLGAKKDGR LTAVKMDFRA NTGPYGNHSL TVPCNGPALS LPLYPCDNVD
     FQVTTYYSNI CPNGAYQGYG APKGNFAITM ALAELAEQLQ IDQLEIIERN RVHEGQELKI
     LGAIGEGKAP TSVPSAASCA LEEILRQGRE MIQWSSPKPQ NGDWHIGRGV AIIMQKSGIP
     DIDQANCMIK LESDGTFIVH SGGADIGTGL DTVVTKLAAE VLHCPPQDVH VISGDTDHAL
     FDKGAYASSG TCFSGNAARL AAENLREKIL FHGAQMLGEP VADVQLATPG VVRGKKGEVS
     FGDIAHKGET GTGFGSLVGT GSYITPDFAF PYGANFAEVA VNTRTGEIRL DKFYALLDCG
     TPVNPELALG QIYGATLRAI GHSMSEEIIY DAEGHPLTRD LRSYGAPKIG DIPRDFRAVL
     VPSDDKVGPF GAKSISEIGV NGAAPAIATA IHDACGIWLR EWHFTPEKIL TALEKI
 
 
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