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YGFK_ECOLI
ID   YGFK_ECOLI              Reviewed;        1032 AA.
AC   Q46811; Q2M9W2;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Putative oxidoreductase YgfK {ECO:0000305};
DE   AltName: Full=Putative oxidoreductase Fe-S subunit {ECO:0000303|PubMed:22094925};
GN   Name=ygfK; OrderedLocusNames=b2878, JW5923;
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   DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=12480890; DOI=10.1099/00221287-148-12-3865;
RA   Bebien M., Kirsch J., Mejean V., Vermeglio A.;
RT   "Involvement of a putative molybdenum enzyme in the reduction of selenate
RT   by Escherichia coli.";
RL   Microbiology 148:3865-3872(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IRON-BINDING, AND PRELIMINARY
RP   FUNCTION.
RX   PubMed=22094925; DOI=10.1039/c1mt00154j;
RA   Sevcenco A.M., Pinkse M.W., Wolterbeek H.T., Verhaert P.D., Hagen W.R.,
RA   Hagedoorn P.L.;
RT   "Exploring the microbial metalloproteome using MIRAGE.";
RL   Metallomics 3:1324-1330(2011).
CC   -!- FUNCTION: Could be an iron-sulfur flavoprotein with NADPH:O(2)
CC       oxidoreductase activity. {ECO:0000305|PubMed:22094925}.
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};
CC   -!- DISRUPTION PHENOTYPE: Insertion mutant is unable to reduce selenate to
CC       selenium. {ECO:0000269|PubMed:12480890}.
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DR   EMBL; U28375; AAA83059.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75916.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76944.1; -; Genomic_DNA.
DR   PIR; F65071; F65071.
DR   RefSeq; NP_417354.1; NC_000913.3.
DR   RefSeq; WP_000502395.1; NZ_LN832404.1.
DR   AlphaFoldDB; Q46811; -.
DR   SMR; Q46811; -.
DR   BioGRID; 4262325; 21.
DR   BioGRID; 853310; 1.
DR   DIP; DIP-28091N; -.
DR   IntAct; Q46811; 2.
DR   STRING; 511145.b2878; -.
DR   PaxDb; Q46811; -.
DR   PRIDE; Q46811; -.
DR   EnsemblBacteria; AAC75916; AAC75916; b2878.
DR   EnsemblBacteria; BAE76944; BAE76944; BAE76944.
DR   GeneID; 949068; -.
DR   KEGG; ecj:JW5923; -.
DR   KEGG; eco:b2878; -.
DR   PATRIC; fig|1411691.4.peg.3856; -.
DR   EchoBASE; EB2873; -.
DR   eggNOG; COG0493; Bacteria.
DR   eggNOG; COG1145; Bacteria.
DR   HOGENOM; CLU_014791_0_0_6; -.
DR   OMA; NECGNCE; -.
DR   BioCyc; EcoCyc:G7497-MON; -.
DR   PRO; PR:Q46811; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0015930; F:glutamate synthase activity; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT   CHAIN           1..1032
FT                   /note="Putative oxidoreductase YgfK"
FT                   /id="PRO_0000201329"
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;  115582 MW;  588056B51BE89648 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 CSPDLTIEQL KNQGFHYVLI ATGTDKNSGV KLAGDNQNVW
     KSLPFLREYN KGTALKLGKH VVVVGAGNTA MDCARAALRV PGVEKATIVY RRSLQEMPAW
     REEYEEALHD GVEFRFLNNP ERFDADGTLT LRVMSLGEPD EKGRRRPVET NETVTLLVDS
     LITAIGEQQD TEALNAMGVP LDKNGWPDVD HNGETRLTDV FMIGDVQRGP SSIVAAVGTA
     RRATDAILSR ENIRSHQNDK YWNNVNPAEI YQRKGDISIT LVNSDDRDAF VAQEAARCLE
     CNYVCSKCVD VCPNRANVSI AVPGFQNRFQ TLHLDAYCNE CGNCAQFCPW NGKPYKDKIT
     VFSLAQDFDN SSNPGFLVED CRVRVRLNNQ SWVLNIDSKG QFNNVPPELN DMCRIISHVH
     QHHHYLLGRV EV
 
 
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