ID A0A179GCE2_PURLI Unreviewed; 935 AA.
AC A0A179GCE2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755};
DE EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755};
GN ORFNames=VFPBJ_09447 {ECO:0000313|EMBL:OAQ75474.1}, VFPFJ_09556
GN {ECO:0000313|EMBL:OAQ81101.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ75474.1, ECO:0000313|Proteomes:UP000078240};
RN [1] {ECO:0000313|EMBL:OAQ75474.1, ECO:0000313|Proteomes:UP000078240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLBJ-1 {ECO:0000313|EMBL:OAQ75474.1}, and PLFJ-1
RC {ECO:0000313|EMBL:OAQ81101.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964}.
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:OAQ75474.1}.
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DR EMBL; LSBH01000008; OAQ75474.1; -; Genomic_DNA.
DR EMBL; LSBI01000009; OAQ81101.1; -; Genomic_DNA.
DR RefSeq; XP_018174945.1; XM_018326625.1.
DR AlphaFoldDB; A0A179GCE2; -.
DR STRING; 33203.A0A179GCE2; -.
DR GeneID; 28891674; -.
DR KEGG; plj:VFPFJ_09556; -.
DR OMA; GECESFA; -.
DR OrthoDB; 1472084at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000078240; Unassembled WGS sequence.
DR Proteomes; UP000078340; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR004352; GH114_TIM-barrel.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR35273; ALPHA-1,4 POLYGALACTOSAMINIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G07890)-RELATED; 1.
DR PANTHER; PTHR35273:SF2; ALPHA-GALACTOSIDASE; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF03537; Glyco_hydro_114; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000078340};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..350
FT /note="Glycoside-hydrolase family GH114 TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF03537"
FT DOMAIN 360..431
FT /note="AMP-activated protein kinase glycogen-binding"
FT /evidence="ECO:0000259|Pfam:PF16561"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 96983 MW; 7BB3782D2E944F75 CRC64;
MSDAEHAAPA ASEKRSGNEN DGGDKTKDKR PGWPLWKKLA VAGAIFLVVV GLAVGLGVGL
TRSRGGGDSD SSDDEKRDGG APPPPSNGTG SSRSSVWRPK AGTSWQIVLK NPVDLGSGGG
GSGVTPDVDV YDLDMYENSA ATFQKLHGAG KKVVCYFSAG SYEDWRADKG EFKDVDLGKP
LRGWAGERWL KLGSENVRRI MSKRVEYAAQ KGCDAIDPDN VDGYQNDNGL GLTANDTISF
VTFLQAEASR HNMSMGLKNA AGIIPEVLHL CDFSVNEQCV EEGECESFAA FVAAGKPVFH
IEYPDGVDGE NAAGGKILKA AAEEICGRKG KAKGAEGFST VMKRMELDGW VEYCDGKVEH
PAEEAYVTGT FDNWQKTVKL EKSDGVFQKT VDIAHPSHKI YYKFVVDNNW TINESSPHEP
DSDGNVNNFL TQADLEHPSF SSSILNTVTP ESTTVAMAGK KNNKKKQQQK AQQAAAATKP
AETAPAETAA AAPVAAEVVP VEAATAEPTA AAATTAAVVE PVVPVAAESR EDTATPSIVP
GGFPETPANE EDKTVSVNPL PAAPGAVNPI TLEPGEKIPQ GVAAQGVNDN VKLDKESYEK
SDALPGVVAT DLPPVSKNTI PESSLPITSN KDATINTVGP GATTAALAGQ VPLESKDAKV
PEVVKESQEK AGVAPEASAV PEEVKEKAAV EEELKSKVQE APGTSEGHAG VGAEKQENTG
LIAGAALTTG GAVAAAAIAA KDKVAETAGP TVNNAAAAAT DAANKNLPDS VKAQLPEAAQ
NHLAAQSKET TLEEVSPQVP AEVKESLTEA GKSPEAAANT EAVVEKKQVE SELLKEVKSV
PAVDETKPAA AAASETKPVA AKAPETKPTE TAATQGKATE ANPEAAKAEA VKAGAANGAN
GTETKPAEAS QPASAQAKKK SRLSTIFSKL KEKLK
//
