ID A0A093YBI3_9PEZI Unreviewed; 1061 AA.
AC A0A093YBI3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=O988_03517 {ECO:0000313|EMBL:KFY00118.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFY00118.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFY00118.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFY00118.1,
RC ECO:0000313|Proteomes:UP000029329};
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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:KFY00118.1}.
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DR EMBL; JPJR01000582; KFY00118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093YBI3; -.
DR HOGENOM; CLU_009402_0_0_1; -.
DR Proteomes; UP000029329; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd11319; AmyAc_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR InterPro; IPR015340; A_amylase_C_dom.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR23501; MAJOR FACILITATOR SUPERFAMILY; 1.
DR PANTHER; PTHR23501:SF107; TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G04730)-RELATED; 1.
DR Pfam; PF09260; A_amylase_dom_C; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 78..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 606..958
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 17..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 114611 MW; 6CB5F8CC64E99DD0 CRC64;
MKLAIFSRVM GERAVAPPVP SPDEVNCETT ASSGKAEKVL VPTEEGERSS DEEAPSETAA
EGIKKVEAIA IVWSRSELYA AYACVFLVYF VNSLQQQITS NLLPYVMSDF ASHSLIPVTG
IVSQILGGVL KLPIAQLINI WGRPQGLIVM TTLCTIGLVL MAVCNNVQTY AAAQCFYWVG
YNGIGFVLDV FIADTSNLRN RALAFAFAST PYIVTTWAGP KAAESFYAHS GWRLGLIQRR
ESGRTVKESL WYYFIEFDVV GILLISAGFA LFLLPFALAG SQTDKWAAAS TIIMLVLGVA
LLAAFGLYEK YLSPRSFIPF HLVTDRTVLG ACGLSAVSFA SFYLWDNYYL SYLQVVHQLS
ITTAGYVFNI FSIGCSFWAV VVAAAIHYTG RIKPLALYFG APLNLLGVGL MIHFRQPSHS
IGYVVMCQIF IAFAGGTLVI CEQMAAMAAV KHADVAAILA VLGLSAAVGG AIGSSMAGAI
WTNTLPDALA AALPEAEKTR SGEIYGSLKE QLAFEWGSEA RKGIVQAYGI AQRRMTIAST
LYFLTRAVKG SSYNKTAVVL RLQIPIRAMF FNRPALVARY LAVAAALFTS TSAKTAAEWR
EASIYQLLTD RFATTEGSAP DCSIRSYCGG TWKGIENKLD YIQGMGFDAI WISPVIHNIE
DNTQYGNAFH GYWGDDPFTL NPHFGAGDDL KSLSDALHGR GMSLMIDVVI NHLAANQPST
SVDYSVFPAP FNSASAFHTP CGIDYTNQGS IENCWLVTDT PSLPDIDSEN GDVYTAMVNS
VADIVKTYGV DGIRLDTARH VPKEFLTQFQ EAVGVFVTGE VLDGNPDFVA GYQGPLSSTL
NYPLWYPLVD SFMGGDFSAL ATTMGTVDSV FTDVNALANF LDNHDQPRFA SREGNDVVRD
RNAATFLMFT SGIPVVYYGF EHRFGGASDP DNREALWGSG YNVDAELYKH IALLHQIRDL
ASGIGEKAAY FSTSAEVIAT SAQYMAIKRG AVVVVVSNVG AQGATDGFNV SGSQFDSGDE
IVDLFSCTTA TVGDGGAFDS TANNGEARIW IRSRDKGSFC P
//
