YLII_ECOLI
ID YLII_ECOLI Reviewed; 371 AA.
AC P75804; Q9R7R6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Aldose sugar dehydrogenase YliI {ECO:0000303|PubMed:16864586};
DE Short=Asd {ECO:0000303|PubMed:16864586};
DE EC=1.1.5.-;
DE AltName: Full=Soluble aldose sugar dehydrogenase YliI;
DE Flags: Precursor;
GN Name=yliI; OrderedLocusNames=b0837, JW0821;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16522795; DOI=10.1110/ps.051889506;
RA Marani P., Wagner S., Baars L., Genevaux P., de Gier J.W., Nilsson I.,
RA Casadio R., von Heijne G.;
RT "New Escherichia coli outer membrane proteins identified through prediction
RT and experimental verification.";
RL Protein Sci. 15:884-889(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 21-370 IN COMPLEX WITH PQQ AND
RP CALCIUM, FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16864586; DOI=10.1074/jbc.m601783200;
RA Southall S.M., Doel J.J., Richardson D.J., Oubrie A.;
RT "Soluble aldose sugar dehydrogenase from Escherichia coli: a highly exposed
RT active site conferring broad substrate specificity.";
RL J. Biol. Chem. 281:30650-30659(2006).
CC -!- FUNCTION: Aldose sugar dehydrogenase with broad substrate specificity.
CC The physiological substrate is unknown. Can oxidize glucose to
CC gluconolactone. Can also utilize D-arabinose, L-arabinose and 2-deoxy-
CC glucose. Has higher activity towards oligomeric sugars, such as
CC maltose, maltotriose or cellobiose. It may function to input sugar-
CC derived electrons into the respiratory network.
CC {ECO:0000269|PubMed:16864586}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16864586};
CC Note=Binds 2 calcium ions per monomer. {ECO:0000269|PubMed:16864586};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16864586}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:16522795}.
CC -!- SIMILARITY: Belongs to the PQQ oxidoreductase GdhB family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC73924.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35540.1; -; Genomic_DNA.
DR PIR; E64821; E64821.
DR RefSeq; NP_415358.1; NC_000913.3.
DR RefSeq; WP_000555031.1; NZ_SSZK01000002.1.
DR PDB; 2G8S; X-ray; 1.50 A; A/B=21-370.
DR PDBsum; 2G8S; -.
DR AlphaFoldDB; P75804; -.
DR SMR; P75804; -.
DR BioGRID; 4261449; 280.
DR IntAct; P75804; 2.
DR STRING; 511145.b0837; -.
DR jPOST; P75804; -.
DR PaxDb; P75804; -.
DR PRIDE; P75804; -.
DR EnsemblBacteria; AAC73924; AAC73924; b0837.
DR EnsemblBacteria; BAA35540; BAA35540; BAA35540.
DR GeneID; 945467; -.
DR KEGG; ecj:JW0821; -.
DR KEGG; eco:b0837; -.
DR PATRIC; fig|1411691.4.peg.1441; -.
DR EchoBASE; EB3253; -.
DR eggNOG; COG2133; Bacteria.
DR HOGENOM; CLU_012253_1_1_6; -.
DR InParanoid; P75804; -.
DR OMA; RLWRIPL; -.
DR PhylomeDB; P75804; -.
DR BioCyc; EcoCyc:G6437-MON; -.
DR BioCyc; MetaCyc:G6437-MON; -.
DR EvolutionaryTrace; P75804; -.
DR PRO; PR:P75804; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005509; F:calcium ion binding; IDA:EcoCyc.
DR GO; GO:0016901; F:oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor; IDA:EcoCyc.
DR GO; GO:0070968; F:pyrroloquinoline quinone binding; IDA:EcoCyc.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR Pfam; PF07995; GSDH; 1.
DR SUPFAM; SSF50952; SSF50952; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell outer membrane; Membrane; Metal-binding;
KW Oxidoreductase; PQQ; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..371
FT /note="Aldose sugar dehydrogenase YliI"
FT /id="PRO_0000025584"
FT REGION 214..215
FT /note="PQQ"
FT REGION 312..314
FT /note="PQQ"
FT REGION 341..343
FT /note="PQQ"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:16864586"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16864586"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16864586"
FT BINDING 261
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:16864586"
FT STRAND 25..42
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2G8S"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2G8S"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2G8S"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 126..137
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:2G8S"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:2G8S"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:2G8S"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:2G8S"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:2G8S"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:2G8S"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:2G8S"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:2G8S"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:2G8S"
SQ SEQUENCE 371 AA; 41054 MW; 99DB08FA302F50B9 CRC64;
MHRQSFFLVP LICLSSALWA APATVNVEVL QDKLDHPWAL AFLPDNHGML ITLRGGELRH
WQAGKGLSAP LSGVPDVWAH GQGGLLDVVL APDFAQSRRI WLSYSEVGDD GKAGTAVGYG
RLSDDLSKVT DFRTVFRQMP KLSTGNHFGG RLVFDGKGYL FIALGENNQR PTAQDLDKLQ
GKLVRLTDQG EIPDDNPFIK ESGARAEIWS YGIRNPQGMA MNPWSNALWL NEHGPRGGDE
INIPQKGKNY GWPLATWGIN YSGFKIPEAK GEIVAGTEQP VFYWKDSPAV SGMAFYNSDK
FPQWQQKLFI GALKDKDVIV MSVNGDKVTE DGRILTDRGQ RIRDVRTGPD GYLYVLTDES
SGELLKVSPR N
