GANAB_DICDI
ID GANAB_DICDI Reviewed; 943 AA.
AC Q94502; Q55DG2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Neutral alpha-glucosidase AB;
DE EC=3.2.1.207;
DE AltName: Full=Alpha-glucosidase 2;
DE AltName: Full=Glucosidase II subunit alpha;
DE AltName: Full=Protein post-translational modification mutant A;
DE Flags: Precursor;
GN Name=modA; Synonyms=ganab; ORFNames=DDB_G0269154;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=AX4;
RX PubMed=9397534;
RX DOI=10.1002/(sici)1520-6408(1997)21:3<177::aid-dvg1>3.0.co;2-4;
RA Freeze H.H., Lammertz M., Iranfar N., Fuller D., Panneerselvam K.,
RA Loomis W.F.;
RT "Consequences of disrupting the gene that encodes alpha-glucosidase II in
RT the N-linked oligosaccharide biosynthesis pathway of Dictyostelium
RT discoideum.";
RL Dev. Genet. 21:177-186(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Cleaves sequentially the 2 innermost alpha-1,3-linked glucose
CC residues from N-linked oligosaccharides on newly synthesized
CC glycoproteins. {ECO:0000250, ECO:0000269|PubMed:9397534}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein] = beta-D-glucose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein] (N-glucan mannose isomer 9A1,2,3B1,2,3);
CC Xref=Rhea:RHEA:56000, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59080,
CC ChEBI:CHEBI:139493; EC=3.2.1.207;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-
CC asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc)-L-asparaginyl-[protein]; Xref=Rhea:RHEA:55996,
CC Rhea:RHEA-COMP:14355, Rhea:RHEA-COMP:14357, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:59080, ChEBI:CHEBI:59082;
CC EC=3.2.1.207;
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:9397534}. Golgi apparatus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 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; U72236; AAB18921.1; -; Genomic_DNA.
DR EMBL; AAFI02000005; EAL71927.1; -; Genomic_DNA.
DR RefSeq; XP_646169.1; XM_641077.1.
DR AlphaFoldDB; Q94502; -.
DR SMR; Q94502; -.
DR STRING; 44689.DDB0191113; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PaxDb; Q94502; -.
DR PRIDE; Q94502; -.
DR EnsemblProtists; EAL71927; EAL71927; DDB_G0269154.
DR GeneID; 8617122; -.
DR KEGG; ddi:DDB_G0269154; -.
DR dictyBase; DDB_G0269154; modA.
DR eggNOG; KOG1066; Eukaryota.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; Q94502; -.
DR OMA; KQENTIY; -.
DR PhylomeDB; Q94502; -.
DR BRENDA; 3.2.1.207; 1939.
DR UniPathway; UPA00957; -.
DR PRO; PR:Q94502; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:dictyBase.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:dictyBase.
DR GO; GO:0090599; F:alpha-glucosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IMP:dictyBase.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IMP:dictyBase.
DR GO; GO:0043687; P:post-translational protein modification; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Golgi apparatus;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..943
FT /note="Neutral alpha-glucosidase AB"
FT /id="PRO_0000328193"
FT REGION 186..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 540
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT ACT_SITE 543
FT /evidence="ECO:0000250"
FT ACT_SITE 617
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 943 AA; 108772 MW; 703DF52FDB23333E CRC64;
MRKLVILIIL SIVCSLFIGS IESVDTSKFK TCKDSHFCKR NRVSHEVGVM NEMKSKQNFN
IVEGSIKLVK QENTIYFDLQ EQNQKSNLLT MKLEIYEGGI VRMRAQEKEP LLNKQRYQVQ
DVLLDTIKTV PIQWKQEPSK QSNTFSFKHG EKECCYVLVQ LVPFKLDVYI MNELAITTNS
DNLFHFEPIS DKPQPLPPKE KKSEEENKEA NQEEDNNNNN NDNNEEQQVS TEGYWEERFG
SHQDSKPNGP MSIGMDFTFV GSSHVYGIPE HTTRLSLKST TGNGINEQPY RLYNLDVFEY
EIDKTMALYG HVPLMISHDT KKTVGVFWLN AAETFVDIED VTTPVSPSKK THWISESGII
DVFYLTGPTP STIFKQYAYL TGTTALPQMF SLGYHQCKWN YKSEDDVKQV DNGFDENHIP
YDVIWLDIEH TDGKRYFTWD NNNFPTPADM QNIIGAKHRK MVTIVDPHIK RDNNYYVHSE
ATSKGYYIKN KDGNDYDGWC WPGSSSYLDF TNPEIRKWWA TQFGYDKYKG STPNLYIWND
MNEPSVFNGP EVSMHKDAKH HGGFEHRDVH NLYGYYYHMA SADGLVQRNA DQNDRPFVLS
RAFYAGSQRI GAIWTGDNSA QWSHLEISNP MLLSMNLAGI TFSGADVGGF FGNPDAELLT
RWYQAGAFQP FFRGHAHLDS RRREPWLFNE PYTTIIREAI VKRYSYLPLW YTTFYQNTLN
GAPVMRPLWV QYPKEANLFD VDDHYLIGDS LLVKPVTQQS CKTMKVLLPG QSVNEIWYDV
DTEKPINAGV IEIDTPLEKI PVYQRGGSII SKKERVRRST YQMRDDPYTI RIALDSSKSA
QGQLYIDDEH SFDYKKGKFL YRQFTFKDNV LSFSDASNKS STSYKPNVTI EKIVILGVQK
PHSITCNITG KEKLSFEYDS TLSKLTIRKP DLLVDTDFII KLN
