ID A0A0J1J2V6_9FIRM Unreviewed; 730 AA.
AC A0A0J1J2V6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=RHS_2766 {ECO:0000313|EMBL:KLU71451.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU71451.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU71451.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU71451.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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:KLU71451.1}.
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DR EMBL; JNGB01000023; KLU71451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1J2V6; -.
DR PATRIC; fig|1504536.3.peg.3307; -.
DR Proteomes; UP000036477; 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; 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; 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.
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:UP000036477}.
FT DOMAIN 30..286
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 650..724
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"
SQ SEQUENCE 730 AA; 83357 MW; FBA05DEA35612B5F CRC64;
MAVTFDQEKK VFSLQTKNAT YQMLVSSYQH LIHVYYGAKI GRMELSYLIR GINRGFSGNP
YEGGNDRGYS LDTYPQEYST FGMGDYRSSC LQAENPDGSQ VTELLYVSHK IYDGKYALEG
LPAVWAEESE AQTLEIVLKD QATDLEVTLL YGVLEDYDVI TRACRIKNGN QDAVYLNRAL
TACLDFTTDH FDVISFYGKH NMERIMQRRN VCHGKVLIDS TRGTSSHHEN PFMIICGRDA
GEEYGECYGA SFVYSGNFMA QVEVDQVNQT RFTMGINADG FRYKLEPGDV FTTPEVILSF
SANGLGTLSG NFHKLYMDHL IRSKFKKQRR PVLINNWEAT EFEFEEDTLV SIADSAKDLG
IELFVMDDGW FGTRNHDLSG LGDWFVNKTK LPSGVTGLAK KINNLGMKFG IWIEPEMVNE
DSDLFRNHPE WCMRIPGRKP NLERFQLVLD ISRQDVRDYL FETIGKILDE ANVEYVKWDM
NRNFADVWSA LLPKDRQGEV CHRYVLGLYD MMEKFVTKYP DILFEGCSGG GGRFDAGMLY
YMPQIWCSDD TDAIERIRIQ YGTSFGYPIS TVGAHVSVSP NQQTGRSTPL ETRGTVAMAG
TFGYELDVRT LDEEEREAVR QQIQFFKENY DLIQYGTYYR LSNPEENRDY AAWQFVNEDG
SKSLFSIVVL HSYANPALFR VRVKGLKPDS FYKVNDEDRI YEGSALMNAG INIPLVNGDY
QSFNFAIKEI
//
