ID   B2UN73_AKKM8            Unreviewed;       798 AA.
AC   B2UN73;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   02-SEP-2026, entry version 85.
DE   RecName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|PROSITE-ProRule:PRU10066};
DE            EC=3.2.1.3 {ECO:0000256|PROSITE-ProRule:PRU10066};
GN   OrderedLocusNames=Amuc_1870 {ECO:0000313|EMBL:ACD05684.1};
OS   Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS   81048 / CCUG 64013 / CIP 107961 / Muc).
OC   Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
OC   Verrucomicrobiales; Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD05684.1, ECO:0000313|Proteomes:UP000001031};
RN   [1] {ECO:0000313|Proteomes:UP000001031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC   / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX   PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA   van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA   Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT   "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT   degrader, and its use in exploring intestinal metagenomes.";
RL   PLoS ONE 6:E16876-E16876(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC         successively from non-reducing ends of the chains with release of
CC         beta-D-glucose.; EC=3.2.1.3; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU10066};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; CP001071; ACD05684.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2UN73; -.
DR   STRING; 349741.Amuc_1870; -.
DR   PaxDb; 349741-Amuc_1870; -.
DR   KEGG; amu:Amuc_1870; -.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_000631_7_2_0; -.
DR   OrthoDB; 176168at2; -.
DR   BioCyc; AMUC349741:G1GBX-1996-MONOMER; -.
DR   Proteomes; UP000001031; Chromosome.
DR   GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06604; GH31_glucosidase_II_MalA; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF120; HETEROGLYCAN GLUCOSIDASE 1; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001031}.
FT   DOMAIN          34..206
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          248..574
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          582..669
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          685..733
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
FT   ACT_SITE        402
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10066"
SQ   SEQUENCE   798 AA;  90914 MW;  71ED95A3988DD09F CRC64;
     MCSVSNIPER RKTPPLRGSL VKWEYTNTVS KITLSVCLAD AGIVRVTYFP GAVPEDEPSY
     AVSPGYSAPG AEIREYDEDG FHVVETSLLR IRIRTEEQKV DFYDVATDEP LLTDEGGFGR
     ESKDWTGDAR VWIRKNLQET EHFFGLGDKP CALNLRGKYF SMWGADHYDF HEESDPLYKS
     IPFFLSLRER KAYGLLFDNT CRSYFDFGAT DEKVLSFGSF GGLMNYYFIY DNTPLDIISA
     YTRLTGTPEL PPLWALGYHQ SKWSYYPDKA VYNLVERFRG LGIPCDAVHL DHHYMERKEG
     FTWDKQNFPD AEGMVRALEK DGVKTVLIVN PGVKVNSVNP VWKEGMERNY FCRRSEGNLL
     SEEVWPGLCN FPDFTAPAVR GWWADLFSRD IGKIGVRGLW NDMNEPVVFP DRTFPMDTRH
     EYDGMPCSHE KAHNIYGQCM AEASWLGMKR HAPDRRPFLL SRSGFAGLQR FAATWTGDNR
     SSWEHLKLAN FQCQRLAASG ISFAGADAGG FMGHPTPELF CRWMQMASFH GFFRNHSSGE
     FGGQEPWVFG QEVTSYVKAA IEGRYRLLPY IYTQFRRYAE TGMPVLRSLA LQCFTNKDTY
     WRGAEYFFGD HLYVIPIHEP QEGGRFLYIP EGVWYSYHTD SLMEDTGKDV WVKCPLSFLP
     VYVRGGAVIP HWPVQQYVGE LPRPPLTLDV WWAPEGEVAS HLYEDAGDGY AYRNGECAVH
     GFLYRGGTNS LELDWNCEGD PCAFHESAEV VLHGLPAGIS VSACMDGVPC CGVMREGRVW
     KIPVKDKFDT LSVCWPEE
//