ID F5IXX8_9BACT Unreviewed; 733 AA.
AC F5IXX8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=HMPREF9455_01945 {ECO:0000313|EMBL:EGK01797.1};
OS Dysgonomonas gadei ATCC BAA-286.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=742766 {ECO:0000313|EMBL:EGK01797.1, ECO:0000313|Proteomes:UP000004913};
RN [1] {ECO:0000313|EMBL:EGK01797.1, ECO:0000313|Proteomes:UP000004913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-286 {ECO:0000313|EMBL:EGK01797.1,
RC ECO:0000313|Proteomes:UP000004913};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dysgonomonas gadei ATCC BAA-286.";
RL Submitted (APR-2011) 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:EGK01797.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADLV01000020; EGK01797.1; -; Genomic_DNA.
DR RefSeq; WP_006799473.1; NZ_GL891982.1.
DR AlphaFoldDB; F5IXX8; -.
DR STRING; 742766.HMPREF9455_01945; -.
DR eggNOG; COG3345; Bacteria.
DR HOGENOM; CLU_009640_2_2_10; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000004913; 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:UP000004913};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..733
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003324124"
FT DOMAIN 47..276
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 642..729
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 472
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 542
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 356..357
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 436
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 470..474
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 520
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 542
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 733 AA; 83067 MW; 4FE02514E6CAECFC CRC64;
MRTSVLSIFL LFLTTLNVFS QEKKVIQVET DNLAMIFTAS PNEKVIFQYW GNKLNGVSSF
TDKKIKGQPD TNDDFASQMY PAYGGRYYLN PALKLTHDDG VLTTELIYVG TQTKTLDSNR
TETVISLKDK LYPVYVDVRF IAYKKENIIA QSVTISHKEK SGIKVENLAS SYIPIHAESY
YLTHFNGTWA AEMQMEEEEL THGLKVIETK KGVRATQSEN PSFLLSLNGP ANEDSGEVYG
GSLAWSGNYK LSFELDETGK LGIVAGMNPF ASTFYLKPEQ KLETPEMILT YSASGVGQLS
RNYHDWARRY ALVHGDKLRP VILNSWEGAY FTFDEKTITD MIDDAAKFGV EMFVLDDGWF
GNKYPRNGDN AGLGDWQVNK KKLPRGINYL ADYAVSKGVK FGIWIEPEMV NPDSELAKNH
PEWIVKSGKR DILPMRNQWL LDLSNPEVQD FVFKTFDDVV SMSKNISYIK WDANRHVDNV
GSDYLPKDEQ THFWYEYVKG LYKVYDRIRA KYPDIEIQLC SSGGGRVEFG ALKYHTEFWA
SDNTNALDRI FIQYGTNLFF PAIATGSHVS TSPNHQTGMI TPLKFRFDVA MSGRLGMELQ
PKDIGDEYEF AVNAIKDYKT IRPIVQFGDL CRLVSPYGKH GWASHMYVSK DKKQSVFFAY
SLKYHGRTTY LETKLKGLDP GKNYRITELN VKPGNSSFSG NGQVFSGDYL MKAGINLNIG
NPFDSTVLLI SQE
//
