ID A0A0H3GGW6_KLEPH Unreviewed; 707 AA.
AC A0A0H3GGW6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 OrderedLocusNames=KPHS_00550 {ECO:0000313|EMBL:AEW58753.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW58753.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW58753.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW58753.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(2012).
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}.
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DR EMBL; CP003200; AEW58753.1; -; Genomic_DNA.
DR RefSeq; WP_004151861.1; NC_016845.1.
DR RefSeq; YP_005224355.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GGW6; -.
DR STRING; 1125630.KPHS_00550; -.
DR GeneID; 11845033; -.
DR KEGG; kpm:KPHS_00550; -.
DR PATRIC; fig|1125630.4.peg.55; -.
DR HOGENOM; CLU_009640_3_1_6; -.
DR Proteomes; UP000007841; Chromosome.
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:UP000007841}.
FT DOMAIN 24..239
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 607..693
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 441
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 329..330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 439..443
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 483
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 505
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 707 AA; 79932 MW; 990C3D2230010DD7 CRC64;
MSDSLIHLQS AGADVVIKTR PFAEIVYWGP HLSHFSPQDA DSLTRPVANG RLDVDSPVTL
MAELGHGLFG APGIEGHRQG LDASPLFTTS EVRHEGQTLT LVSEDPQAGL RLQSEIALDA
SGVLSVRHGV TNLRASPWQV DRLAVTLPVA ERAREVMAFH GRWIREFQPH RLTLEHDSFV
LENRRGRTSH EHFPALITGS RAFSEMQGEV WGVHLAWSGN HRLRAEVKTD GRRYLQAEAL
YLPGEMALAE GETLWTPYLY ASYSANGLNG MSQQFHRYLR ERIIRFPGNK PRPVHLNTWE
GIYFDHDPDY IMRMADEAAA LGVERFIIDD GWFKGRNDDW AALGDWYLDE KKYPYGLTPV
IDHVKSLGME FGIWVEPEMI NPDSDLYRAH PDWVLALPGY TPLTGRHQFV LNLNIPEAFD
YLLERMSWLL GEHAVDYVKW DMNRELVQPG HQGRAAADAQ TRQFYRLLDT LVARFPHIEF
ESCSSGGGRI DYEVLKRSHR FWASDNNDAL ERNTIQRGMS YFFPPEVMGA HIGNRHCHAT
FRQHSIAFRG LTALFGHMGL ELDPVSADEE ERAGYRKYAA LHKQWRDVIH HGVQWRIDMP
DATTLAHGVV SPDKAQAIFL VSQLAMPDYT LMAPLRLAGL EASARYQVTL LDHPNIQITG
EGGHTMRKLP AWMTTPQTVS GEWLQQAGLA LPILDPESAI LIGLQRV
//
