ID A0A0G3AQS8_9ACTN Unreviewed; 682 AA.
AC A0A0G3AQS8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168};
DE EC=3.2.1.22 {ECO:0000256|RuleBase:RU361168};
DE AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN ORFNames=ABB07_33435 {ECO:0000313|EMBL:AKJ14787.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ14787.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ14787.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
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|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; CP011497; AKJ14787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3AQS8; -.
DR STRING; 665007.ABB07_33435; -.
DR PATRIC; fig|665007.5.peg.7067; -.
DR Proteomes; UP000035366; Chromosome.
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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.120.1060; NPCBM/NEW2 domain; 1.
DR InterPro; IPR018905; A-galactase_NEW3.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR InterPro; IPR038637; NPCBM_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR Pfam; PF08305; NPCBM; 1.
DR Pfam; PF10633; NPCBM_assoc; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SMART; SM00776; NPCBM; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..682
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005183751"
FT DOMAIN 537..682
FT /note="Glycosyl hydrolase family 98 putative carbohydrate-
FT binding module"
FT /evidence="ECO:0000259|SMART:SM00776"
FT REGION 466..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 70973 MW; 074A57A85AD2DE6D CRC64;
MRHPHTGTPR TTRTTRRRVV GALTAGLLCA AGLAGPALAA PTQDPAAPAA PALADGLALT
PPMGFNNWNS THCRADFDES MVKGIADLFV AKGLKDAGYQ YVNLDDCWAL PQRDAAGKLV
PDPARFPNGI KAVADYVHSK GLKLGIYTSA GTKTCNSAGF PGALGHEYSD ARQFADWGVD
YLKYDNCNNQ GVDAKQRYTT MRDALKATGR PIVYSICEWG ENKPWQWASG VGHLWRTTGD
ISDSWGSMLS ILKQNLPLAP YAGPGHWNDP DMLEVGNGGM TDTEYRSHFS LWSVMAAPLL
IGTDLRKASP ATFGILANKE VVAVDQDPLG KQGTVVSSAG GRWVIAKEMK DGSRAVALFN
ESGTAQRIAT TAAAVGLPDA SAYTLRDLWE HRSYNTAGTI AAAVPAHGTV LLRVSADSHW
AAYPPAAELG LDGSPLVAAG TPATLTSTVT DLGRTAARQV SVSLTGPDGW TVRPTSPTSA
PALGTGGTLR TGWSVTAPPG TATGSYGLTL QARYLSPSGQ GVTSTLPLTA SVVVRPPAGT
SYLSDLPWLS ATSGWGPVER DTSNGESAAG DGHPITIGGT VYAKGLGVHA PSDVSFYTGK
ACDKVTADVG VDDEKGAKGT VTFEIWADGT KVASTGVLTN TMPAQPLTAG ITGAQVIDLV
VTDAGDGNDS DHADWAKVQV SC
//
