ID A0A179T2E5_9BACI Unreviewed; 743 AA.
AC A0A179T2E5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=A6K24_20380 {ECO:0000313|EMBL:OAS87520.1};
OS Metabacillus litoralis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Metabacillus.
OX NCBI_TaxID=152268 {ECO:0000313|EMBL:OAS87520.1, ECO:0000313|Proteomes:UP000078534};
RN [1] {ECO:0000313|Proteomes:UP000078534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C44 {ECO:0000313|Proteomes:UP000078534};
RA Lyu Z., Lyu W.;
RL Submitted (APR-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 ECO:0000256|PIRNR:PIRNR005536};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC {ECO:0000256|PIRNR:PIRNR005536}.
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:OAS87520.1}.
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DR EMBL; LWSG01000009; OAS87520.1; -; Genomic_DNA.
DR RefSeq; WP_066330249.1; NZ_LWSG01000009.1.
DR AlphaFoldDB; A0A179T2E5; -.
DR STRING; 152268.A6K24_20380; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000078534; 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 Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR038417; Alpga-gal_N_sf.
DR InterPro; IPR002252; Glyco_hydro_36.
DR InterPro; IPR031705; Glyco_hydro_36_C.
DR InterPro; IPR031704; Glyco_hydro_36_N.
DR InterPro; IPR013780; Glyco_hydro_b.
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.
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:UP000078534}.
FT DOMAIN 30..286
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 650..739
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 479
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 549
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 367..368
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 477..481
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 743 AA; 85939 MW; C98103F5B0D1577D CRC64;
MTIKVNVETL EFHIFNENVS YIFRVLEKSN QLEHLYYGKK IRHRDSFKHL LEREIRPSCN
MFEDDHTSTL EHIKQEYPSY GTTDYRSPAH MITNKIGSHI TNYQYQSYEI IAGKPKLHQL
PATYVEDENE ANTLEITLWD EVLKSKVILS YTIYKNRNVI CRNTRFVNEG NDAFYINNAM
SASVDLPDDQ FEMVHLNGAW AREAHVDSQK LFKGIQSVYS TRGASSHAHN PFLALKRLDA
TEHTGEVYGF SLVYSGNFLA QVEVDTYSVS RVLIGINPFQ FKWKLNPNET FQTPECVMVY
SDQGLNGMSQ TYHELFRERL VRGYWRDKVR PILINNWEAT YFDFNEEKIV DIASTANNLG
IELFVLDDGW FGERHDDTSS LGDWFENKDK LPNGIKGLSE KIEDLGMKFG LWFEPEMVSK
GTKLFEEHPD WIISTPERRA SHGRNQFVLD FSRAEVVNHI FTLMDNIIND SKISYIKWDM
NRYITEAYST SLKSDQQGEL FHRYILGVYE LYERLIAKYP EILFESCAGG GARFDPGLLY
YAPQAWASDN TDAVERLKIQ YGTSMVYPLS AIGSHISAIP NHQVGRMTSI DTRANVAYFG
TFGYELDITK LGNEEKAKVQ KQVAFFKEKR SLVRSGDFHR LLSPFESNEV SWMVVSKDKT
EALVGYYKVL AKPNDKYYRL KLKGLDSDKL YAIEGIKSTH YGDELMNLGI VLGEDYTDRA
SEFWSREHPH DYASKLFVLK VVN
//
