ID I1BGP8_RHIO9 Unreviewed; 604 AA.
AC I1BGP8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00012593};
DE EC=3.2.1.3 {ECO:0000256|ARBA:ARBA00012593};
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase {ECO:0000256|ARBA:ARBA00033473};
DE AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00033442};
GN ORFNames=RO3G_00082 {ECO:0000313|EMBL:EIE75378.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE75378.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE75378.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC successively from non-reducing ends of the chains with release of
CC beta-D-glucose.; EC=3.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001863};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC {ECO:0000256|ARBA:ARBA00006188}.
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DR EMBL; CH476732; EIE75378.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BGP8; -.
DR STRING; 246409.I1BGP8; -.
DR VEuPathDB; FungiDB:RO3G_00082; -.
DR eggNOG; ENOG502QPM2; Eukaryota.
DR InParanoid; I1BGP8; -.
DR OMA; DALYQWE; -.
DR OrthoDB; 1586242at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005976; P:polysaccharide metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.2440; Carbohydrate binding type-21 domain; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR000165; Glucoamylase.
DR InterPro; IPR046966; Glucoamylase_active_site.
DR PANTHER; PTHR31616:SF11; GLUCOAMYLASE, INTRACELLULAR SPORULATION-SPECIFIC; 1.
DR PANTHER; PTHR31616; TREHALASE; 1.
DR Pfam; PF03370; CBM_21; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR PRINTS; PR00736; GLHYDRLASE15.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51159; CBM21; 1.
DR PROSITE; PS00820; GLUCOAMYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..604
FT /note="glucan 1,4-alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003637331"
FT DOMAIN 26..130
FT /note="CBM21"
FT /evidence="ECO:0000259|PROSITE:PS51159"
FT REGION 127..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 65089 MW; 80F00054261E6B5B CRC64;
MQLFNLPLKV SFFLVLSYFS LLVSAASIPS SASVQLDSYN YDGSTFSGKI YVKNIAYSKK
VTVIYADGSD NWNNNGNTIA ASYSAPISGS NYEYWTFSAS INGIKEFYIK YEVSGKTYYD
NNNSANYQVS TSKPTTTTAT ATTTTAPSTS TTTPPSSSEP ATFPTGNSTI SSWIKKQEGI
SRFAMLRNIN PPGSATGFIA ASLSTAGPDY YYAWTRDAAL TSNVIVYEYN TTLSGNKTIL
NVLKDYVTFS VKTQSTSTVC NCLGEPKFNP DGSGYTGAWG RPQNDGPAER ATTFILFADS
YLTQTKDASY VTGTLKPAIF KDLDYVVNVW SNGCFDLWEE VNGVHFYTLM VMRKGLLLGA
DFAKRNGDST RASTYSSTAS TIANKISSFW VSSNNWIQVS QSVTGGVSKK GLDVSTLLAA
NLGSVDDGFF TPGSEKILAT AVAVEDSFAS LYPINKNLPS YLGNSIGRYP EDTYNGNGNS
QGNPWFLAVT GYAELYYRAI KEWIGNGGVT VSSISLPFFK KFDSSATSGK KYTVGTSDFN
NLAQNIALAA DRFLSTVQLH AHNNGSLAEE FDRTTGLSTG ARDLTWSHAS LITASYAKAG
APAA
//
