ID B8MQX4_TALSN Unreviewed; 584 AA.
AC B8MQX4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|RuleBase:RU361168};
DE EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|RuleBase:RU361168};
DE AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN ORFNames=TSTA_053270 {ECO:0000313|EMBL:EED12809.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED12809.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC more complex molecules such as oligosaccharides and polysaccharides.
CC {ECO:0000256|ARBA:ARBA00003969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00001255,
CC ECO:0000256|RuleBase:RU361168};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
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DR EMBL; EQ962659; EED12809.1; -; Genomic_DNA.
DR RefSeq; XP_002486920.1; XM_002486875.1.
DR AlphaFoldDB; B8MQX4; -.
DR STRING; 441959.B8MQX4; -.
DR GeneID; 8098278; -.
DR VEuPathDB; FungiDB:TSTA_053270; -.
DR eggNOG; KOG2366; Eukaryota.
DR HOGENOM; CLU_013093_3_3_1; -.
DR InParanoid; B8MQX4; -.
DR OMA; NWARFMC; -.
DR OrthoDB; 1217107at2759; -.
DR PhylomeDB; B8MQX4; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR11452:SF90; ALPHA-GALACTOSIDASE A-RELATED; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 437..561
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 584 AA; 65303 MW; D69D1AF922D7B76A CRC64;
MNSHKQYTSG LQVVAVITAV SGWLLPECRA SIENPGLLPT PPMGFNGWSR FQCNINETIF
TQTADAMIST GLQAAGYNRI NLDDCWMADS RTDQNTLTWN TTTFPHGLPW LGSYLTERGF
YFGIYEDAGN VTCGGYPGSY NYEAIDAETF ASWGIDYLKV DGCNVSPGTE AEYHERYSTW
HEVFNNMSSP LIFSQSAPAY FSKWITGSDN LTDWYTTMDY MPYNGELARH SSDIIVYALN
ATSWDGVTSP WGSIMQNYVY EIQLARYQVP GYYNDPDFLI ADHPGLSLDE KKSQFALWAS
FSAPLIISAW IPGLQEDVLS YLKNSDLIAI DQDKLAQQAT LVSRDGAFDV FSKSLDNSDR
LVTVLNLGNT TSSTSISVPR IGLVEELLGV KVEYTAKDLW TGKTIIFQNK LEIKDLASHA
TAVYRISLSA ILSELVIPTG LIFNDASFNC LTAESSNEKN TQIAFNTCSG ADEQVWQIRP
LVGTVSPLSD TSLCLTARNK QAKLERCAVI PLDLYQQWDY SVRGYLTNRL TKECVTESTQ
STLSTCQYED NSQIAFQVTI SHGFFLRRSL FIYHIPTKPL DIYR
//
