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
//