位置:首页 > 蛋白库 > GUTQ_ECOLI
GUTQ_ECOLI
ID   GUTQ_ECOLI              Reviewed;         321 AA.
AC   P17115; Q2MAC1; Q46874;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 3.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Arabinose 5-phosphate isomerase GutQ;
DE            Short=API;
DE            Short=G-API;
DE            EC=5.3.1.13 {ECO:0000269|PubMed:16199563};
DE   AltName: Full=Phosphosugar aldol-ketol isomerase;
GN   Name=gutQ; Synonyms=srlQ; OrderedLocusNames=b2708, JW5431;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-313.
RC   STRAIN=K12;
RX   PubMed=2134185; DOI=10.3109/10425179009016042;
RA   Yamada M., Yamada Y., Saier M.H. Jr.;
RT   "Nucleotide sequence and expression of the gutQ gene within the glucitol
RT   operon of Escherichia coli.";
RL   DNA Seq. 1:141-145(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-6.
RC   STRAIN=K12 / JM109 / ATCC 53323;
RX   PubMed=17366475; DOI=10.1002/pmic.200600599;
RA   Maillet I., Berndt P., Malo C., Rodriguez S., Brunisholz R.A., Pragai Z.,
RA   Arnold S., Langen H., Wyss M.;
RT   "From the genome sequence to the proteome and back: evaluation of E. coli
RT   genome annotation with a 2-D gel-based proteomics approach.";
RL   Proteomics 7:1097-1106(2007).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   NOMENCLATURE.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=16199563; DOI=10.1128/jb.187.20.6936-6942.2005;
RA   Meredith T.C., Woodard R.W.;
RT   "Identification of GutQ from Escherichia coli as a D-arabinose 5-phosphate
RT   isomerase.";
RL   J. Bacteriol. 187:6936-6942(2005).
CC   -!- FUNCTION: Catalyzes the reversible aldol-ketol isomerization between D-
CC       ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). It
CC       appears that the physiological function of G-API may be to synthesize
CC       the regulatory molecule A5P, which in turn participates in the
CC       induction of the gut operon through an unknown mechanism. It is also
CC       able of sustaining the biosynthetic pathway of 3-deoxy-D-manno-
CC       octulosonate (KDO), a unique 8-carbon sugar component of
CC       lipopolysaccharides (LPSs). {ECO:0000269|PubMed:16199563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinose 5-phosphate = D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:23104, ChEBI:CHEBI:57693, ChEBI:CHEBI:58121;
CC         EC=5.3.1.13; Evidence={ECO:0000269|PubMed:16199563};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23105;
CC         Evidence={ECO:0000269|PubMed:16199563};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23106;
CC         Evidence={ECO:0000269|PubMed:16199563};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.64 mM for Ru5P (at pH 8.25 and at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:16199563};
CC         KM=1.2 mM for A5P (at pH 8.25 and at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:16199563};
CC       pH dependence:
CC         Optimum pH is 8.25. {ECO:0000269|PubMed:16199563};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16199563}.
CC   -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69217.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA35745.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA35745.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U29579; AAA69217.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC75750.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76785.1; -; Genomic_DNA.
DR   EMBL; X51361; CAA35745.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_417188.4; NC_000913.3.
DR   RefSeq; WP_001287420.1; NZ_LN832404.1.
DR   AlphaFoldDB; P17115; -.
DR   SMR; P17115; -.
DR   BioGRID; 4263273; 290.
DR   IntAct; P17115; 2.
DR   STRING; 511145.b2708; -.
DR   jPOST; P17115; -.
DR   PaxDb; P17115; -.
DR   PRIDE; P17115; -.
DR   EnsemblBacteria; AAC75750; AAC75750; b2708.
DR   EnsemblBacteria; BAE76785; BAE76785; BAE76785.
DR   GeneID; 947587; -.
DR   KEGG; ecj:JW5431; -.
DR   KEGG; eco:b2708; -.
DR   PATRIC; fig|511145.12.peg.2799; -.
DR   EchoBASE; EB0966; -.
DR   eggNOG; COG0517; Bacteria.
DR   eggNOG; COG0794; Bacteria.
DR   HOGENOM; CLU_040681_13_1_6; -.
DR   InParanoid; P17115; -.
DR   OMA; MPRVITP; -.
DR   PhylomeDB; P17115; -.
DR   BioCyc; EcoCyc:EG10973-MON; -.
DR   BioCyc; MetaCyc:EG10973-MON; -.
DR   PRO; PR:P17115; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
DR   GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR   CDD; cd05014; SIS_Kpsf; 1.
DR   Gene3D; 3.10.580.10; -; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR004800; KdsD/KpsF-type.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035474; SIS_Kpsf.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01380; SIS; 1.
DR   PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   TIGRFAMs; TIGR00393; kpsF; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS51464; SIS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; CBS domain; Direct protein sequencing; Isomerase;
KW   Lipopolysaccharide biosynthesis; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Repeat; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:17366475"
FT   CHAIN           2..321
FT                   /note="Arabinose 5-phosphate isomerase GutQ"
FT                   /id="PRO_0000136572"
FT   DOMAIN          34..177
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   DOMAIN          203..261
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          269..321
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   BINDING         49..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         68..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141..143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            52
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000250"
FT   SITE            104
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000250"
FT   SITE            145
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000250"
FT   SITE            186
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  34031 MW;  85C31DFBD92F7B7C CRC64;
     MSEALLNAGR QTLMLELQEA SRLPERLGDD FVRAANIILH CEGKVVVSGI GKSGHIGKKI
     AATLASTGTP AFFVHPAEAL HGDLGMIESR DVMLFISYSG GAKELDLIIP RLEDKSIALL
     AMTGKPTSPL GLAAKAVLDI SVEREACPMH LAPTSSTVNT LMMGDALAMA VMQARGFNEE
     DFARSHPAGA LGARLLNKVH HLMRRDDAIP QVALTASVMD AMLELSRTGL GLVAVCDAQQ
     QVQGVFTDGD LRRWLVGGGA LTTPVNEAMT VGGTTLQSQS RAIDAKEILM KRKITAAPVV
     DENGKLTGAI NLQDFYQAGI I
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024