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YJHC_ECOLI
ID   YJHC_ECOLI              Reviewed;         372 AA.
AC   P39353; Q2M632;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Uncharacterized oxidoreductase YjhC;
DE            EC=1.-.-.-;
GN   Name=yjhC; OrderedLocusNames=b4280, JW5769;
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=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [2]
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   [3]
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   [4]
RP   INDUCTION.
RX   PubMed=23935044; DOI=10.1128/jb.00692-13;
RA   Kalivoda K.A., Steenbergen S.M., Vimr E.R.;
RT   "Control of the Escherichia coli sialoregulon by transcriptional repressor
RT   NanR.";
RL   J. Bacteriol. 195:4689-4701(2013).
CC   -!- INTERACTION:
CC       P39353; P30750: metN; NbExp=3; IntAct=EBI-542024, EBI-541886;
CC   -!- INDUCTION: Negatively regulated by the transcriptional repressor NanR.
CC       Induced by N-acetylneuraminate, via inactivation of NanR.
CC       {ECO:0000269|PubMed:23935044}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97176.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U14003; AAA97176.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77236.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78274.1; -; Genomic_DNA.
DR   PIR; S56505; S56505.
DR   RefSeq; NP_418700.2; NC_000913.3.
DR   RefSeq; WP_000611568.1; NZ_SSUV01000014.1.
DR   PDB; 6O15; X-ray; 1.35 A; A/B=1-372.
DR   PDBsum; 6O15; -.
DR   AlphaFoldDB; P39353; -.
DR   SMR; P39353; -.
DR   BioGRID; 4261650; 8.
DR   BioGRID; 853090; 2.
DR   DIP; DIP-12617N; -.
DR   IntAct; P39353; 2.
DR   STRING; 511145.b4280; -.
DR   jPOST; P39353; -.
DR   PaxDb; P39353; -.
DR   PRIDE; P39353; -.
DR   EnsemblBacteria; AAC77236; AAC77236; b4280.
DR   EnsemblBacteria; BAE78274; BAE78274; BAE78274.
DR   GeneID; 948808; -.
DR   KEGG; ecj:JW5769; -.
DR   KEGG; eco:b4280; -.
DR   PATRIC; fig|1411691.4.peg.2423; -.
DR   EchoBASE; EB2433; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_16_0_6; -.
DR   InParanoid; P39353; -.
DR   OMA; AAPWSWE; -.
DR   PhylomeDB; P39353; -.
DR   BioCyc; EcoCyc:G7901-MON; -.
DR   BioCyc; MetaCyc:G7901-MON; -.
DR   PRO; PR:P39353; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016836; F:hydro-lyase activity; IDA:EcoCyc.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IMP:EcoCyc.
DR   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Oxidoreductase; Reference proteome.
FT   CHAIN           1..372
FT                   /note="Uncharacterized oxidoreductase YjhC"
FT                   /id="PRO_0000091781"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           11..20
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          26..32
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   TURN            34..36
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           37..44
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           52..56
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           74..82
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           97..110
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           119..122
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           124..135
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          140..151
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           164..167
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           169..173
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           176..185
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          190..197
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          211..218
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          224..252
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   TURN            253..256
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          257..262
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          265..269
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   STRAND          271..274
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           275..286
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           305..322
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           329..334
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           338..356
FT                   /evidence="ECO:0007829|PDB:6O15"
FT   HELIX           362..366
FT                   /evidence="ECO:0007829|PDB:6O15"
SQ   SEQUENCE   372 AA;  41384 MW;  34B2E535EADC2ABE CRC64;
     MINYGVVGVG YFGAELARFM NMHDNAKITC VYDPENGENI ARELQCINMS SLDALVSSKL
     VDCVIVATPN YLHKEPVIKA AKNKKHVFCE KPIALSYEDC VDMVKACKEA GVTFMAGHIM
     NFFNGVQYAR KLIKEGVIGE ILSCHTKRNG WENKQERLSW KKMKEQSGGH LYHHIHELDC
     VQHLLGEIPE TVTMIGGNLA HSGPGFGNED DMLFMTLEFP SGKLATLEWG SAFNWPEHYV
     IINGTKGSIK IDMQETAGSL RIGGQTKHFL VHETQEEDDD RRKGNMTSEM DGAIAYGHPG
     KKTPLWLASL IRKETLFLHN ILCGAKPEED YIDLLNGEAA MSAIATADAA TLSRSQDRKV
     KISEIIKHTS VM
 
 
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