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YGFK_ECO57
ID   YGFK_ECO57              Reviewed;        1032 AA.
AC   Q8XD75;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Putative oxidoreductase YgfK {ECO:0000250|UniProtKB:Q46811};
GN   Name=ygfK; OrderedLocusNames=Z4217, ECs3751;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Could be an iron-sulfur flavoprotein with NADPH:O(2)
CC       oxidoreductase activity. {ECO:0000250|UniProtKB:Q46811}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711};
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DR   EMBL; AE005174; AAG58007.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37174.1; -; Genomic_DNA.
DR   PIR; C85943; C85943.
DR   PIR; G91097; G91097.
DR   RefSeq; NP_311778.1; NC_002695.1.
DR   RefSeq; WP_000502397.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XD75; -.
DR   SMR; Q8XD75; -.
DR   STRING; 155864.EDL933_4079; -.
DR   EnsemblBacteria; AAG58007; AAG58007; Z4217.
DR   EnsemblBacteria; BAB37174; BAB37174; ECs_3751.
DR   GeneID; 916425; -.
DR   KEGG; ece:Z4217; -.
DR   KEGG; ecs:ECs_3751; -.
DR   PATRIC; fig|386585.9.peg.3913; -.
DR   eggNOG; COG0493; Bacteria.
DR   eggNOG; COG1145; Bacteria.
DR   HOGENOM; CLU_014791_0_0_6; -.
DR   OMA; NECGNCE; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR017701; Se_rdtase_YgfK.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   TIGRFAMs; TIGR03315; Se_ygfK; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT   CHAIN           1..1032
FT                   /note="Putative oxidoreductase YgfK"
FT                   /id="PRO_0000201330"
FT   DOMAIN          928..958
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         938
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         941
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         944
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         948
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ   SEQUENCE   1032 AA;  115563 MW;  C032E7D2956E738C CRC64;
     MGDIMRPIPF EELLTRIFDE YQQQRSIFGI PEQQFYSPVK GKTVSVFGET CATPVGPAAG
     PHTQLAQNIV TSWLTGGRFI ELKTVQILDR LELEKPCIDA EDECFNTEWS TEFTLLKAWD
     EYLKAWFALH LLEAMFQPSD SGKSFIFNMS VGYNLEGIKQ PPMQQFIDNM MDASDHPKFA
     QYRDTLNKLL QDDAFLARHG LQEKRESLQA LPARIPTSMV HGVTLSTMHG CPPHEIEAIC
     RYMLEEKGLN TFVKLNPTLL GYARVREILD VCGFGYIGLK EESFDHDLKL TQALEMLERL
     MALAKEKSLG FGVKLTNTLG TINNKGALPG EEMYMSGRAL FPLSINVAAV LSRAFDGKLP
     ISYSGGASQL TIRDIFDTGI RPITMATDLL KPGGYLRLSA CMRELEGSDA WGLDHVDVER
     LNRLAADALT MEYTQKHWKP EERIEVAEDL PLTDCYVAPC VTACAIKQDI PEYIRLLGEH
     RYADALELIY QRNALPAITG HICDHQCQYN CTRLDYDSAL NIRELKKVAL EKGWDEYKQR
     WHKPAGSGSR HPVAVIGAGP AGLAAGYFLA RAGHPVTLFE REANAGGVVK NIIPQFRIPA
     ELIQHDIDFV AAHGVKFEYG CSPDLTVEQL KNQDFHYVLI ATGTDKNSGV KLAGDNQNVL
     KSLPFLREYN KGTALKLGKH VVVVGAGNTA MDCARAALRV PGVEKATVVY RRSLQEMPAW
     REEYEEALHD GVEFRFLNNP ERFDADGTLT LRVMSLGEPD EKGRRRPVET NETVTLHVDS
     LITAIGEQQD TEALNAMGVP LDKNGWPDVD HNGETRLTDV FMIGDVQRGP SSIVAAVGTA
     RRATDAILSR ENIRSHQNDK YWNNVNPAEI YQRKGDISIT LVNSDDRDAF VAQEAARCLE
     CNYVCSKCVD VCPNRANVSI AVPGFQNRFQ TLHLDAYCNE CGNCAQFCPW NGKPYKDKIT
     VFSLAQDFDN SSNPGFLVED CRVRVRLNNQ SWVLNIDSEG QFNNVPPELN DMCRIISHVH
     QHHHYLLGRV EV
 
 
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