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Database: UniProt
Entry: M3K385_CANMX
LinkDB: M3K385_CANMX
Original site: M3K385_CANMX 
ID   M3K385_CANMX            Unreviewed;      1756 AA.
AC   M3K385;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:EMG49189.1};
GN   ORFNames=G210_0124 {ECO:0000313|EMBL:EMG49189.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG49189.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG49189.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMG49189.1}.
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DR   EMBL; AOGT01000786; EMG49189.1; -; Genomic_DNA.
DR   STRING; 1245528.M3K385; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   eggNOG; KOG1154; Eukaryota.
DR   eggNOG; KOG2063; Eukaryota.
DR   HOGENOM; CLU_239223_0_0_1; -.
DR   OrthoDB; 3680211at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0046352; P:disaccharide catabolic process; IEA:UniProt.
DR   GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04242; AAK_G5K_ProB; 1.
DR   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR   CDD; cd21157; PUA_G5K; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   HAMAP; MF_00456; ProB; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR041739; G5K_ProB.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR   InterPro; IPR019797; Glutamate_5-kinase_CS.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   NCBIfam; TIGR01027; proB; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF01472; PUA; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          950..1217
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
SQ   SEQUENCE   1756 AA;  200973 MW;  4FE433DA10E01344 CRC64;
     MHDPKWWKEA IVYQIWPASY KDSNDDGVGD IPGIISTLDY LKDLGTDVVW LSPMYDSPQD
     DMGYDISDYE NVYPKYGTLD NMQELINGCH KRGMKLILDL VINHTSDQHE WFKESRSSKD
     NPKRDWYIWK PPKIDADGKR HPPNNWGSYF SGSTWKYDEL TGEYYLHLFA ESQPDLNWEN
     KECREAIYKS ALKFWLEKGV DGFRIDTAGM YSKHQDFKDA PVVLPDVEFQ PCKIYHQHGP
     RIHEFHKEIA EIMAPYDTMT VGEVGHSTKD QSLKYVSAEA KEMNMMFLFD AVEIGSDPRD
     RFRYHGFDLV DFKKAIKSQG EFIEGTDAWS TVFLENHDQP RSISRFGNDS PEYRVASGKT
     LAMLQCCLTG TEFIYQGQEI GMINVPKTWD IKEYLDINTI NYYNQFKDTA SKEKLDQLLV
     NINLLARDNA RTPVQWTDQE NAGFSGRKPW MKTNDSYKEI NVAKELENKD SLLNFWKQMI
     KIRKEYKDLF VYGGFEILDI EDPKLFKFVK TGDNNRKALV VLNFSTDEVA FTYNGKISVS
     TQTPTEDEVT REPRLANMAL IVETMVKLRR QGHKIVIVSS GAIAFGMKRV GLDEKPSKLS
     AVQALASIGQ GRLIGLFDDL FRQLEQPIAQ ILITRNDIMD FTQYKNAKNT VNELLEMGII
     PIVNENDTLS VSEIKFGDND TLSAITAGMI HADYLFLMTD VECLYTDNPR TNPDAEPILI
     VDKIDELHVK TDTEDGGAGS KVGTGGMTTK LIAAELATNI GVTTIITLSS KPYSILDIVA
     HIQEQSSELL TIEQQRDAMK RDVKSGRLPL HTRFLSLPQA TQIKSDRRFW LLHGLKTRGA
     LIIDQGCFQA LTRKNRAGLL PAGILEVVGQ FHESECVSIK VVADKNYLED AVEVGHCRVN
     YSAPEIRLIK GHKSSEIESI LGYADMVYDD LAKIDYRISP ILENLSLLDD EVITTISTYE
     NNIYLGTSIG NLLHFHKFED STEYIGITTL EVSPHSISKI ICVPDIQRLI LVSNRVTAAY
     TLPELSPCHM KKMKDVNDLY HLDTDRILVL SPTKLRIIRL QQDQISLSRE INYANGTTVK
     SSSSHKSNYI VVANNQNYDI IDLENNRKVP LFDYKTDTTS DIQPIIVPFD DEYLLTVSSD
     TSTSMAMFIS TAGDVTRGTL TWVDEGYPQG GIVIESSYVF ALFNKKIIVS SLDSLESVVQ
     MDYDNDDANR IIKVDQAFIE DEESKELIGS TIQPIPAHIV LTNGKSVLGV HRKHKLVELQ
     QQVLNVLENQ GDWKSLQIDP TEFTGELESY AYHLLLLQSI VTNNEVTTLQ VLNRENNGVL
     EISPDFVTYL IGEGEKPEIF HGLEPILEKW TFSKDTELLK KYIRNLKQDY LSDKLQLLYY
     EISSDTESLD FIKSKNWTTY DEHVKSIIEL LTKKDRFVCV SEIFKSLGLI DDYVIFLNAH
     LSNDILDDTI QLVLSEKLNE SQYAKTLINI INFDKPKGYE VLRKAPKKYQ AINNSIMKDL
     SAEDSNQDRS FALLQVELME KAFKENSNLQ DELFELLRSI LKLMYEEVKD DFDLLHTEFL
     QMNSLEKNKW PKIPWLDFLR ICGKSKDLAI FVDFYLKSFE LQEGKITDDP IFVYHRLFTK
     SDIPGLLEYG DYTTAERLAS GENPYPKKYF YKEFTFTPTE PNEEKLRQVL TFYLSKYTSN
     EPVAYAVKHF AETYSKNIPI LDFLNLIPDN FPIAYLTDYF KITIKDINET YRDGIMTKSI
     AKAEALRTRK LSKDLS
//
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