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Arabinose 5-phosphate isomerase GutQ (API) (G-API) (EC 5.3.1.13) (Phosphosugar aldol-ketol isomerase)

 GUTQ_ECOLI              Reviewed;         321 AA.
P17115; Q2MAC1; Q46874;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
11-JUL-2001, sequence version 3.
28-MAR-2018, entry version 142.
RecName: Full=Arabinose 5-phosphate isomerase GutQ;
Short=API;
Short=G-API;
EC=5.3.1.13;
AltName: Full=Phosphosugar aldol-ketol isomerase;
Name=gutQ; Synonyms=srlQ; OrderedLocusNames=b2708, JW5431;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-313.
STRAIN=K12;
PubMed=2134185; DOI=10.3109/10425179009016042;
Yamada M., Yamada Y., Saier M.H. Jr.;
"Nucleotide sequence and expression of the gutQ gene within the
glucitol operon of Escherichia coli.";
DNA Seq. 1:141-145(1990).
[4]
PROTEIN SEQUENCE OF 2-6.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=17366475; DOI=10.1002/pmic.200600599;
Maillet I., Berndt P., Malo C., Rodriguez S., Brunisholz R.A.,
Pragai Z., Arnold S., Langen H., Wyss M.;
"From the genome sequence to the proteome and back: evaluation of E.
coli genome annotation with a 2-D gel-based proteomics approach.";
Proteomics 7:1097-1106(2007).
[5]
FUNCTION AS A ARABINOSE 5-PHOSPHATE ISOMERASE, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, AND NOMENCLATURE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=16199563; DOI=10.1128/JB.187.20.6936-6942.2005;
Meredith T.C., Woodard R.W.;
"Identification of GutQ from Escherichia coli as a D-arabinose 5-
phosphate isomerase.";
J. Bacteriol. 187:6936-6942(2005).
-!- FUNCTION: Catalyzes the reversible aldol-ketol isomerization
between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate
(A5P). It appears that the physiological function of G-API may be
to synthesize the regulatory molecule A5P, which in turn
participates in the induction of the gut operon through an unknown
mechanism. It is also able of sustaining the biosynthetic pathway
of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar
component of lipopolysaccharides (LPSs).
{ECO:0000269|PubMed:16199563}.
-!- CATALYTIC ACTIVITY: D-arabinose 5-phosphate = D-ribulose 5-
phosphate.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.64 mM for Ru5P (at pH 8.25 and at 37 degrees Celsius)
{ECO:0000269|PubMed:16199563};
KM=1.2 mM for A5P (at pH 8.25 and at 37 degrees Celsius)
{ECO:0000269|PubMed:16199563};
pH dependence:
Optimum pH is 8.25. {ECO:0000269|PubMed:16199563};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16199563}.
-!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA69217.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA35745.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA35745.1; Type=Frameshift; Positions=214; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U29579; AAA69217.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC75750.2; -; Genomic_DNA.
EMBL; AP009048; BAE76785.1; -; Genomic_DNA.
EMBL; X51361; CAA35745.1; ALT_SEQ; Genomic_DNA.
RefSeq; NP_417188.4; NC_000913.3.
RefSeq; WP_001287420.1; NZ_LN832404.1.
ProteinModelPortal; P17115; -.
SMR; P17115; -.
BioGrid; 4263273; 290.
IntAct; P17115; 2.
STRING; 316385.ECDH10B_2876; -.
PaxDb; P17115; -.
PRIDE; P17115; -.
EnsemblBacteria; AAC75750; AAC75750; b2708.
EnsemblBacteria; BAE76785; BAE76785; BAE76785.
GeneID; 947587; -.
KEGG; ecj:JW5431; -.
KEGG; eco:b2708; -.
PATRIC; fig|511145.12.peg.2799; -.
EchoBASE; EB0966; -.
EcoGene; EG10973; gutQ.
eggNOG; ENOG4105C2X; Bacteria.
eggNOG; COG0517; LUCA.
eggNOG; COG0794; LUCA.
HOGENOM; HOG000264729; -.
InParanoid; P17115; -.
KO; K02467; -.
OMA; MSEAVIQ; -.
PhylomeDB; P17115; -.
BioCyc; EcoCyc:EG10973-MONOMER; -.
BioCyc; MetaCyc:EG10973-MONOMER; -.
PRO; PR:P17115; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IMP:UniProtKB.
CDD; cd05014; SIS_Kpsf; 1.
InterPro; IPR000644; CBS_dom.
InterPro; IPR004800; KdsD/KpsF-type.
InterPro; IPR001347; SIS.
InterPro; IPR035474; SIS_Kpsf.
Pfam; PF00571; CBS; 1.
Pfam; PF01380; SIS; 1.
PIRSF; PIRSF004692; KdsD_KpsF; 1.
TIGRFAMs; TIGR00393; kpsF; 1.
PROSITE; PS51371; CBS; 2.
PROSITE; PS51464; SIS; 1.
1: Evidence at protein level;
ATP-binding; CBS domain; Complete proteome; Direct protein sequencing;
Isomerase; Lipopolysaccharide biosynthesis; Metal-binding;
Nucleotide-binding; Reference proteome; Repeat; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:17366475}.
CHAIN 2 321 Arabinose 5-phosphate isomerase GutQ.
/FTId=PRO_0000136572.
DOMAIN 34 177 SIS. {ECO:0000255|PROSITE-
ProRule:PRU00797}.
DOMAIN 203 261 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 269 321 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
NP_BIND 49 54 ATP. {ECO:0000255}.
REGION 68 69 Substrate binding. {ECO:0000250}.
REGION 107 116 Substrate binding. {ECO:0000250}.
REGION 141 143 Substrate binding. {ECO:0000250}.
METAL 75 75 Zinc. {ECO:0000250}.
BINDING 75 75 Substrate. {ECO:0000250}.
BINDING 81 81 Substrate. {ECO:0000250}.
BINDING 215 215 Substrate. {ECO:0000250}.
BINDING 267 267 Substrate. {ECO:0000250}.
SITE 52 52 Catalytically relevant. {ECO:0000250}.
SITE 104 104 Catalytically relevant. {ECO:0000250}.
SITE 145 145 Catalytically relevant. {ECO:0000250}.
SITE 186 186 Catalytically relevant. {ECO:0000250}.
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


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