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 27-MAR-2024, entry version 126. 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; Pseudomonadota; 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}. 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; 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 CAZy; GH13; Glycoside Hydrolase Family 13. 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 OrthoDB; 9805159at2; -. DR BRENDA; 3.2.1.20; 5347. DR Proteomes; UP000001976; Chromosome. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC. DR CDD; cd11330; AmyAc_OligoGlu; 1. DR Gene3D; 3.20.20.80; Glycosidases; 2. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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 PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1. DR PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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 //