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Database: UniProt
Entry: Q6D270_PECAS
LinkDB: Q6D270_PECAS
Original site: Q6D270_PECAS 
ID   Q6D270_PECAS            Unreviewed;       453 AA.
AC   Q6D270;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   SubName: Full=6-phospho-alpha-glucosidase {ECO:0000313|EMBL:CAG76124.1};
DE            EC=3.2.1.122 {ECO:0000313|EMBL:CAG76124.1};
GN   OrderedLocusNames=ECA3226 {ECO:0000313|EMBL:CAG76124.1};
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG76124.1, ECO:0000313|Proteomes:UP000007966};
RN   [1] {ECO:0000313|EMBL:CAG76124.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG76124.1};
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA   Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA   Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA   Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA   Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT   "The genome sequence of the enterobacterial phytopathogen Erwinia
RT   carotovora subsp. atroseptica SCRI1043 and functional genomic
RT   identification of novel virulence factors.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU361152};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC       {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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DR   EMBL; BX950851; CAG76124.1; -; Genomic_DNA.
DR   RefSeq; WP_011094747.1; NC_004547.2.
DR   AlphaFoldDB; Q6D270; -.
DR   STRING; 218491.ECA3226; -.
DR   GeneID; 57209910; -.
DR   KEGG; eca:ECA3226; -.
DR   PATRIC; fig|218491.5.peg.3268; -.
DR   eggNOG; COG1486; Bacteria.
DR   HOGENOM; CLU_045951_2_0_6; -.
DR   OMA; TWRNIKP; -.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0050081; F:maltose-6'-phosphate glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05298; GH4_GlvA_pagL_like; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR32092:SF14; MALTOSE-6'-PHOSPHATE GLUCOSIDASE; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW   Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007966}.
FT   DOMAIN          197..419
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        173
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   ACT_SITE        268
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         202
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   SITE            111
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   453 AA;  50806 MW;  3FC957041765C8F3 CRC64;
     MTKPPFILTI AGGGSTYTPG IVKSLMVRLA DFPLAEIRLY DIDGQRQDII APVVEKVIRD
     HSDSIVFTVT TDAETAFTGA HFVFAQMRVG QYKMREQDEK IPLRHGVVGQ ETCGPGGLAY
     GLRTILPMAE LIDLVERYAH KDAWIVNYSN PAAIVAEGVR RLRPNARVLN ICDMPVAAMR
     NIAAVLGVDR HDITVDYFGL NHFGWFTRVL VDGVDRMPEL REHIARYGLL TADAADTDPQ
     HADPSWVKTW RNIKPIMDHF PEFVPNPYLQ YYLMPNQIVE HQDPDYTRAN EVMDGREKKL
     FAAAASYKET GILPDAFHVG VHGSFIVDVA CSLAFDLRQR HLVIVENKGA IANLPYDAMV
     EVPAYITAQG PEPVRMGNVP QFHRALLEQQ LASEQLLVEA TLEGSYEKAL QAFTLNRTVP
     TMQHAKAILD DMIEANQDYW PQLKQAYRDG IAQ
//
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