ID   AGLA_RHIME              Reviewed;         551 AA.
AC   Q9Z3R8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Probable alpha-glucosidase;
DE            EC=3.2.1.20;
GN   Name=aglA; OrderedLocusNames=R00698; ORFNames=SMc03064;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10400573; DOI=10.1128/jb.181.14.4176-4184.1999;
RA   Willis L.B., Walker G.C.;
RT   "A novel Sinorhizobium meliloti operon encodes an alpha-glucosidase and a
RT   periplasmic-binding-protein-dependent transport system for alpha-
RT   glucosides.";
RL   J. Bacteriol. 181:4176-4184(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; AF045609; AAD12047.1; -; Genomic_DNA.
DR   EMBL; AL591688; CAC45270.1; -; Genomic_DNA.
DR   RefSeq; NP_384804.1; NC_003047.1.
DR   AlphaFoldDB; Q9Z3R8; -.
DR   SMR; Q9Z3R8; -.
DR   STRING; 266834.SMc03064; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q9Z3R8; -.
DR   EnsemblBacteria; CAC45270; CAC45270; SMc03064.
DR   KEGG; sme:SMc03064; -.
DR   PATRIC; fig|266834.11.peg.2073; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_3_5; -.
DR   OMA; PNGEKWA; -.
DR   BRENDA; 3.2.1.20; 5347.
DR   Proteomes; UP000001976; Chromosome.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..551
FT                   /note="Probable alpha-glucosidase"
FT                   /id="PRO_0000054312"
FT   ACT_SITE        212
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            345
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        13
FT                   /note="P -> A (in Ref. 1; AAD12047)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20..21
FT                   /note="GA -> RP (in Ref. 1; AAD12047)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402..415
FT                   /note="YGIQFWPDFKGRDG -> MASSSGPTSSAGR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        445..460
FT                   /note="PRAVAVQEGDPASVLH -> RGRCRAGGRPGLGAA (in Ref. 1;
FT                   AAD12047)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  62576 MW;  BB7BD3E17C935509 CRC64;
     MTMNETTSSL LEPDRDWWRG AVIYQIYPRS FQDTNGDGIG DLQGITARLP HIAGLGADAI
     WISPFFTSPM RDFGYDVSNY VDVDPIFGTL EDFDALIAEA HRLGLRVMID LVLSHTSDRH
     PWFVESRSSR SNAKADWYVW ADSKPDGTPP NNWLSIFGGS AWQWDPTRLQ YYLHNFLTSQ
     PDLNLHNPQV QEALLAVERF WLERGVDGFR LDTINFYFHD RELRDNPALV PERRNASTAP
     AVNPYNYQEH IYDKNRPENL EFLKRFRAVM DEFPAIAAVG EVGDSQRGLE IAGEYTSGGD
     KVHMCYAFEF LAPDRLTPQR VAEVLRDFHR AAPEGWACWA FSNHDVVRHV SRWADGVTDH
     DAHAKLLASL LMSLRGTVCI YQGEELALAE AELDYEDLQD PYGIQFWPDF KGRDGCRTPM
     VWESLPDGGF SSATPWLPIS QSHIPRAVAV QEGDPASVLH HYRRFLAFRK ANPALAKGEI
     EFVETRGSLL GFLRSHGNEK VFCLFNMSDE AATKELPMKR LEPLEGHGFV SEILDHEVKL
     PAWGAFFARL A