ID A0A0J9UPJ5_FUSO4 Unreviewed; 785 AA.
AC A0A0J9UPJ5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=FOXG_04689 {ECO:0000313|EMBL:KNB01449.1};
OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS / NRRL 34936) (Fusarium vascular wilt of tomato).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=426428 {ECO:0000313|EMBL:KNB01449.1, ECO:0000313|Proteomes:UP000009097};
RN [1] {ECO:0000313|EMBL:KNB01449.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4287 {ECO:0000313|EMBL:KNB01449.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KNB01449.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4287 {ECO:0000313|EMBL:KNB01449.1};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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 ECO:0000256|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; DS231699; KNB01449.1; -; Genomic_DNA.
DR RefSeq; XP_018239494.1; XM_018382718.1.
DR AlphaFoldDB; A0A0J9UPJ5; -.
DR GeneID; 28946715; -.
DR KEGG; fox:FOXG_04689; -.
DR VEuPathDB; FungiDB:FOXG_04689; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000009097; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 2.60.40.2440; Carbohydrate binding type-21 domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF03370; CBM_21; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000009097};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..785
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005324227"
FT DOMAIN 26..127
FT /note="CBM21"
FT /evidence="ECO:0000259|PROSITE:PS51159"
FT REGION 128..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 84674 MW; 3F6C633F547B398A CRC64;
MRFLPSTLFV WLLLTIKILA APSNSAHEKR ATQVSLKSYT YTGSTLAGSV KIQNIAYAKA
VSVYWAAGST WMSTPISASY STGPDSSGYE TWTFSGTAAS ATQFYIAYIV SGTTYYDPGN
NVNYQITSST SKTSTSTTGT STRASSTITS STTSSSTVPA GTGGTVSPSS IPPFYSATIP
TEAAATAPTG CGNFNGKDSC ASGSTYTVPD SAENRRWQTP PKGDTAYFDT FQSYRSLTGY
ADIQYSSSKT SAAVVINCLS RTDETLTYSF NGANQTSNVY QANQSTKGGL TIVVYGSSGS
VLTLDPLYFL WENAVISGQQ SSFSDGQKGA IVELFGWPYT DIAKECSFLS KAGYMGLKIW
PPQEHVWGSN YYEPDNQFRP WYFVYQPVSY RLQSRLGSRA ELRAMIQTCR AVGVRVYFDA
VLNHMSGNGN DVQNHRNTDC SLYTGHNGTA GSPFYTWGQT YLINPFSGTR PTVEFPAVPY
GPTDFHCERS LSSWTDGQVI TKGWLVGLTD LNSEKPYVQD RVATYLVDVL SLGASGFRVD
AAKHIGPAMM AQIYKRVKQK LGGGDFPADF ISWNEVILGG EKDLLACGGG EWSWYTNFDN
VLSAAGLSST DIAKIKIWSS DYPKEFPACG SWVIPASRFA IQNDDHDQQS PGSSSRDMGD
SGSVLIKDKD ISKHRAFEVQ LFSRTDGDWK IKLVLSSYMF ASNGASGFPD GKSDCSLYTG
SQSQSGCLGM AYDQAYVASA CGYGGGTLMA GKYTRVHRDL SIINAMRAWV GLGSTTALAL
GISGC
//
