ID A0A094CGQ6_9PEZI Unreviewed; 590 AA.
AC A0A094CGQ6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glycosyl hydrolase family 13 catalytic domain-containing protein {ECO:0000259|SMART:SM00642};
GN ORFNames=V496_07886 {ECO:0000313|EMBL:KFY53119.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY53119.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY53119.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
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:KFY53119.1}.
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DR EMBL; JPJY01001510; KFY53119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CGQ6; -.
DR STRING; 1420909.A0A094CGQ6; -.
DR HOGENOM; CLU_006462_2_3_1; -.
DR OrthoDB; 3680211at2759; -.
DR Proteomes; UP000029302; Unassembled WGS sequence.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
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; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF232; GLYCOSYL HYDROLASE FAMILY 13 CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 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 Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302}.
FT DOMAIN 30..445
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 440..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 67725 MW; 3272791393EA24B5 CRC64;
MTSKIISSQE TYARYDAQPR AWWKEASVYQ IYPASFCDTT GNGIGDIRGI ISKMDYIKTL
GVDVVWLCPI FASPQIDMGY DISDYKTINP QYGTIEDVDT LMNGLHKRGV KLLLDLVVNH
TSDQHEWFNQ SKSGKDNPYR DWYIWRTPKY DKEGNRQPPN NWVSHFEGSA WEYDEASDEY
YLHLFAKEQP DLNWEHKPVR DAVHEIMRFW LSRGIDGFRL DVINYISKPQ DFPDSSQPPD
GVLGTEFYCA GPRLHEYLQD VGAILNEYNA FSVGEMPSVQ DLNEVIKAVR YNRNELNMIF
HFDFMCLDKG ADDKYSPRTW KLTELKAPVT KWQRFMYDNG GWNALYLENH DQPRSVSRFA
CDSPKYRTQS AKMLATFLAF QAGTVFIYEG QELGMTNVPK GWPLDEYKDI SCLNHQQWLK
TQTTDETAFA IAREEYQKKS RDNARTPMQW TSNVNSGGFS SSSNPTWMKV NPNTELINAA
AQIDDPSSPF SYWKVVLAAR KEYKDSFIYG DFEMLDENDE KVLAYTRKAE DGTTILVLCN
FSAEETPWSL KSEVGSAKKV VLSNSGKTLD DFICGNVALA AYEACVVLLE
//