GenomeNet

Database: UniProt
Entry: R5FC01_9BACT
LinkDB: R5FC01_9BACT
Original site: R5FC01_9BACT 
ID   R5FC01_9BACT            Unreviewed;       531 AA.
AC   R5FC01;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=BN812_01931 {ECO:0000313|EMBL:CCY02418.1};
OS   Prevotella sp. CAG:924.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262938 {ECO:0000313|EMBL:CCY02418.1, ECO:0000313|Proteomes:UP000018357};
RN   [1] {ECO:0000313|EMBL:CCY02418.1, ECO:0000313|Proteomes:UP000018357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:924 {ECO:0000313|Proteomes:UP000018357};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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|RuleBase:RU361168};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC       {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
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:CCY02418.1}.
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; CAXK010000104; CCY02418.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5FC01; -.
DR   STRING; 1262938.BN812_01931; -.
DR   Proteomes; UP000018357; Unassembled WGS sequence.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd04081; CBM35_galactosidase-like; 1.
DR   CDD; cd14792; GH27; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002241; Glyco_hydro_27.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR041233; Melibiase_C.
DR   PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE MEL1; 1.
DR   PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF16499; Melibiase_2; 1.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51175; CBM6; 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   Reference proteome {ECO:0000313|Proteomes:UP000018357};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..531
FT                   /note="Alpha-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004379432"
FT   DOMAIN          399..531
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
SQ   SEQUENCE   531 AA;  58878 MW;  EC61E68310835ABD CRC64;
     MNKHFLLLLL ALSSVVTAWG KSFVPPTMGW SSWNTYFARI SDGLIRRQTD ALVSTGLSRV
     GYRYVNIDDG FFAGRDAKGN LLINTSKFPG GLKPVVEYIH GKGLKAGIYT DAGHNTCASF
     YNGEPGGVGA GIYEHEAQDC RLYFDSLKFD FIKVDFCGGN APQNSEHLAL DPQTRYTDIA
     KAIKATGRDV VYNVCRWDFP GTWVCKMANS WRISQDINNS WGSVANIIRQ NMYLSAYCSP
     GHYNDMDMLE VGRGMTDTED QTHFAMWCIM SSPLLIGCDL TTASDKTLKL LGNEDLIAVN
     QDSLGLQAYV ACVKDGVYTL VKDFRKRNST TRVIAVYNPT DIQKTVDVSF QDVCLGGNVK
     VYDLIDKSKE TCAGQMKVTV AAHGVRVFQL TGKKRLMRRC YEAETAYLSD YQELQNNQAV
     GTAVYEEQAG CSGGMKVGWL GGKASNDLQW RDVYVPKGGT YSMTLSVISG ESRDMYCEVN
     GKAYGKLTCN TGDWSTVKKY KMEVKLKAGN NVIRLYNASS NMPDIDCMYL E
//
DBGET integrated database retrieval system