ID A0A167LE68_PHYB8 Unreviewed; 697 AA.
AC A0A167LE68;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
DE EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
GN ORFNames=PHYBLDRAFT_171639 {ECO:0000313|EMBL:OAD70257.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD70257.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR005536}.
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|PIRNR:PIRNR005536};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC {ECO:0000256|PIRNR:PIRNR005536}.
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DR EMBL; KV440989; OAD70257.1; -; Genomic_DNA.
DR RefSeq; XP_018288297.1; XM_018436638.1.
DR AlphaFoldDB; A0A167LE68; -.
DR STRING; 763407.A0A167LE68; -.
DR GeneID; 28997544; -.
DR VEuPathDB; FungiDB:PHYBL_171639; -.
DR InParanoid; A0A167LE68; -.
DR OrthoDB; 1217107at2759; -.
DR Proteomes; UP000077315; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd14791; GH36; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.70.98.60; alpha-galactosidase from lactobacil brevis; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR038417; Alpga-gal_N_sf.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR002252; Glyco_hydro_36.
DR InterPro; IPR031705; Glyco_hydro_36_C.
DR InterPro; IPR031704; Glyco_hydro_36_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR Pfam; PF16874; Glyco_hydro_36C; 1.
DR Pfam; PF16875; Glyco_hydro_36N; 1.
DR Pfam; PF02065; Melibiase; 1.
DR PIRSF; PIRSF005536; Agal; 1.
DR PRINTS; PR00743; GLHYDRLASE36.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR005536};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005536};
KW Reference proteome {ECO:0000313|Proteomes:UP000077315}.
FT DOMAIN 34..259
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 617..692
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 450
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 518
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 448..452
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 496
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 697 AA; 78569 MW; FD366B7A60EAA2A6 CRC64;
MIPLGVSQHP SSNTWFIVSN SSTYVIGATS EGVVLNLHWG GRLHFYNDVS SANLPIPRSS
QDPALTAIAE EMPAYGGLRY GAIGLKAEIT STQTRELELL WTKAEFQSNQ LKITLCDKAY
PLFSVELVYT VDIDNDVISR HTIIKNRTEI KIHLSKAYSA VWHLPTILGK RKLTTLTGAW
AAETQVNTEN LVNGTLVLES RRGIPSCQTY PYVALQDQEE VYFGTLGWSG SWAIEVHTGW
DGKVTIAGGV HEHDFGWSLF PNMTYETPVF VAGYSVTGLS GARSSLTNHV RNLQRNSMTV
NPIIFNSWET TQFEASYENQ LHQATKAAAV GVELFVLDDG WFRGRTSDRS GLGDWFADPV
KFPQGLKPLA DQVHRLGMKF GLWFEPEMVN RDSDLFRAHP DWVYHYTDRT SSESRNQLVL
NITRPEVEDY VYKRISETIR QVGVDYIKWD MNRPLSEVTM STYRDAREVW VRHVQTWYSL
LERLRRDFPL VLVETCSSGG GRADIGALEL TDMCWPSDNT RPDARLVVQH GISHALPPRV
LGCWVTEGLT PLSYRFHTAF MGNLGIGCDL NRTGVRLEDF KDWIDIYKTL RHIIQLGNLD
WLIGPGQINV TATSLDDEMV VLALREHSPY GLLLPPVRIQ GLVASYLYRV HVWSNDPKKK
TSYTISGACA MQIGLPLDWL AQADYGSGVM HLKRILL
//