GenomeNet

Database: UniProt
Entry: A0A196N3L0_9SPHN
LinkDB: A0A196N3L0_9SPHN
Original site: A0A196N3L0_9SPHN 
ID   A0A196N3L0_9SPHN        Unreviewed;       631 AA.
AC   A0A196N3L0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=A7X12_22325 {ECO:0000313|EMBL:OAN62232.1};
OS   Sphingomonas sp. TDK1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=453247 {ECO:0000313|EMBL:OAN62232.1, ECO:0000313|Proteomes:UP000078445};
RN   [1] {ECO:0000313|EMBL:OAN62232.1, ECO:0000313|Proteomes:UP000078445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TDK1 {ECO:0000313|EMBL:OAN62232.1,
RC   ECO:0000313|Proteomes:UP000078445};
RA   Takahashi S.;
RT   "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT   strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT   Bacteria.";
RL   Submitted (MAY-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|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:OAN62232.1}.
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; LXVY01000027; OAN62232.1; -; Genomic_DNA.
DR   RefSeq; WP_064312330.1; NZ_LXVY01000027.1.
DR   AlphaFoldDB; A0A196N3L0; -.
DR   STRING; 453247.A7X12_22325; -.
DR   OrthoDB; 9807519at2; -.
DR   Proteomes; UP000078445; Unassembled WGS sequence.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd14792; GH27; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.120.1060; NPCBM/NEW2 domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR   InterPro; IPR002241; Glyco_hydro_27.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR041233; Melibiase_C.
DR   InterPro; IPR038637; NPCBM_sf.
DR   PANTHER; PTHR11452:SF80; ALPHA-GALACTOSIDASE 1; 1.
DR   PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR   Pfam; PF16499; Melibiase_2; 2.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   Pfam; PF08305; NPCBM; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SMART; SM00776; NPCBM; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..631
FT                   /note="Alpha-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008272610"
FT   DOMAIN          489..631
FT                   /note="Glycosyl hydrolase family 98 putative carbohydrate-
FT                   binding module"
FT                   /evidence="ECO:0000259|SMART:SM00776"
SQ   SEQUENCE   631 AA;  67937 MW;  AA9C2E4E024AE7EA CRC64;
     MAIKTLAGIS ALLLASASVQ AAPRDPLAPT GRWSANTDGR AATPPMGWNS WNAFATDVDE
     EKVLASAQKI VDTGLAAKGY RYVNLDEGWW DHRRTDGRML VRADKFPSAR TADGATSFKP
     FTDRLHAMGL KAGIYTDLGR NTCAQAYGPN EPNLPRGSVP EREVGLYGHI DQDIALYFGA
     WGFDYIKIDG CGLRAYGEDS PLVRAGRYRP LAPILDLDSV NRSNIPAVRA MFAQVKAALV
     RADPDQDYLL SLCIWGSADV RSWAKDVGNI SRTSDDITPH WTRLLTNFDT AARRPLYAHP
     GSWNDPDMLF IGKGEFDADH LTEARSHFAL WAMVSAPLLI GADLRTTPQA LMDIFGNAAL
     ISVDQDPAGN QAVLAYDSDD FQILVKTLAD GDKAVALFNR TAAPMEAILT AQHLKLRDDA
     AIALTDLWSG ASSSFRKEAK FKLAPHETLV FRARGPRLLT DGLYLSEMPG SVNPAADGIT
     APMADPTIHR AVVSWSGTRG AGQRPLYAGW GGAQADATPY GRELAVAGKH FTAGLGVLAN
     SRLEVRNAGY RQLSVSVGVD DSATDAAHAV TFQIYGDRRL LATAAPVRRG APAKPLSVNV
     AGVKLVELVA RSAGVVNEQL PIVWGDAAFH R
//
DBGET integrated database retrieval system