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Database: UniProt
Entry: A0A098QZP7_9SPIO
LinkDB: A0A098QZP7_9SPIO
Original site: A0A098QZP7_9SPIO 
ID   A0A098QZP7_9SPIO        Unreviewed;       774 AA.
AC   A0A098QZP7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=DC28_04125 {ECO:0000313|EMBL:KGE73325.1};
OS   Spirochaeta lutea.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE73325.1, ECO:0000313|Proteomes:UP000029692};
RN   [1] {ECO:0000313|EMBL:KGE73325.1, ECO:0000313|Proteomes:UP000029692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC230 {ECO:0000313|EMBL:KGE73325.1,
RC   ECO:0000313|Proteomes:UP000029692};
RA   Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT   "De novo Genome Sequence of Spirocheata sp.";
RL   Submitted (MAY-2014) 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:KGE73325.1}.
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DR   EMBL; JNUP01000031; KGE73325.1; -; Genomic_DNA.
DR   RefSeq; WP_052078432.1; NZ_JNUP01000031.1.
DR   AlphaFoldDB; A0A098QZP7; -.
DR   STRING; 1480694.DC28_04125; -.
DR   eggNOG; COG3345; Bacteria.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000029692; 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:UP000029692}.
FT   DOMAIN          97..322
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          688..771
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   REGION          44..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        515
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        576
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         403..404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         480
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         513..517
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         554
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         576
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ   SEQUENCE   774 AA;  85974 MW;  249FD49D642C4ECC CRC64;
     MIQLHDRQAI IHAGPLTYSL GATPEGFLLQ GFAGYLGSGV HSFQGDSNAS ASEASPDPSG
     QNLPFQYLGP SARKAYHPPR PNSCAGQIYA PDIEPAQALM PPDLGPDSEL WEFPAPGIGD
     FRNPGIEIRT GEGHTTCDLR VRSMRLLDEK PAIKGLPSVR QNPLEGDRTL EILLEDRVLS
     LEIRLLYTSL PEYGVIARSA RVHNKGSRVL HLGHLASLNL DLPIHDYYFG QLSGTWARER
     HPLFRPLQPG LTEVHSRRGQ SGPETSPQIF LAAPGTTETT GEVFSAGLVY SGNFSGSAEV
     NGFGATRLQI GINPRGFDWP LAPGESFQAP EAWLGYSNRG FGPLSRNLHR LIRERLCISP
     WSSRERPILL NNWEATYFDF SHKDLVTLAK AGAKAGIELF VLDDGWFGER RNDSSSLGDW
     EVNPQKLPRG LEGLAGDIRA LGLEFGLWIE PEMVSPDSQL YRRHPDWCIH IPGRNRTLGR
     NQLVLDLARR EVQDWIIHTV EGLVSKAPIT YIKWDMNRPI TESSPAHSHS YMLGLYRILE
     HLTLGHPEVL FEGCSAGGGR FDLGMLAYYP QFWTSDDTDA IERLPIQWGT SLGYPTSAMA
     SHISAVPNHQ VGRTTPLDTR AVTAFWGVFG YELNLSRSKD EELTQLNTLS GWYKKLRTLL
     QFGDLYRLEG PTARPLGCSS PGALDRWSWM MTSRDRGRAL VCSVQVLSQP NPTVPRFLRL
     EGLNAKTMYR VWAVSPRGQE DLGLVPGEVA LYRGIALPYR PGDFQSAMLY LEES
//
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