ID A0A261FD95_9BIFI Unreviewed; 839 AA.
AC A0A261FD95;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755};
DE EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755};
GN ORFNames=AEAE_0155 {ECO:0000313|EMBL:OZG56846.1};
OS Aeriscardovia aeriphila.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Aeriscardovia.
OX NCBI_TaxID=218139 {ECO:0000313|EMBL:OZG56846.1, ECO:0000313|Proteomes:UP000228976};
RN [1] {ECO:0000313|EMBL:OZG56846.1, ECO:0000313|Proteomes:UP000228976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21773 {ECO:0000313|EMBL:OZG56846.1,
RC ECO:0000313|Proteomes:UP000228976};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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 -!- 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:OZG56846.1}.
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DR EMBL; MWWU01000001; OZG56846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FD95; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000228976; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:InterPro.
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; 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; PF16875; Glyco_hydro_36N; 1.
DR Pfam; PF02065; Melibiase; 1.
DR PRINTS; PR00743; GLHYDRLASE36.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000228976}.
FT DOMAIN 49..297
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT REGION 754..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 91062 MW; 0FAE4542BD38227D CRC64;
MTELTSSAGV RIVSLNDTTL DGQHSLQGVY LESDNGEVGV ALVARDKELP RLVHWGRALA
HPRHVLHLYE AQRPQRVSGE LDDTTWPSIL PTQAEAWIGA KRLDIRRGTR ELFLNFELQE
ITTTLIDPAQ GDGLDAELDP GAAGGVQVNV IARDSAQNIA VNWRLQMLPG GLIRQSARLV
NNEPMASGEN NGADNLEISK VELGWPLPSR ASEVLTTTGH HLHERRAQRQ KLSMSRIEKV
AMAGRPDFDF SLLLAAGTPG FSFEEGEVYV EHLGWSGNSV MAAEKLPYCE PQISGAELLY
GGEVSLEPGD TYATPWLYGS YGNGLNEASK RYHRFVRAAH PCFAQVQRPV LLNTWEAVYF
EHSYATLAAL ADKAADAGVE RFVVDDGWFM HRRSDNAGLG DWSVDPAVWP EGEHSLKALA
DHVHAKGMQF GLWFEPEMIN PDSDTARAHP EWILRASASN QPGSELGRLP MQGRNQQVID
LTNPAAYEHV FNAMDTLVSQ LHIDYIKWDH NKLVTEPISP YSGRPAVHEQ TRAVYSIFQG
LKKNHPGLEI ESCSSGGGRI DLGMLRFADR VWVSDCVDPV EREENQRWDS VIVPPEILGE
HIGKSPADST KRATSLSLRA AMAFFGHLGV EWNLLTVPAE QLEQLAVWVD AYKALRPLFS
TGMVVHSGPD DSDEPAAYVD GVVAQDGSKA VYRFTQLTAS RSYPAEPVRL PGLNPRSLYR
VSLLPASVAD MPEKGNGQSD LLWAVGGGAR GGAAGARGGA AGAGASSKSA VSEGEVSEVS
SKSAVSEGEV SEVSSASPVS PAFSGSVTLD GEALSRYGIR PPSLHPAQAV LFVVDEVEE
//