ID A0A1X1MQE1_9VIBR Unreviewed; 700 AA.
AC A0A1X1MQE1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=ST37_14760 {ECO:0000313|EMBL:ORT49622.1};
OS Vibrio sp. qd031.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1603038 {ECO:0000313|EMBL:ORT49622.1, ECO:0000313|Proteomes:UP000193432};
RN [1] {ECO:0000313|EMBL:ORT49622.1, ECO:0000313|Proteomes:UP000193432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORT49622.1, ECO:0000313|Proteomes:UP000193432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA Chen G.;
RT "Denovo assembling a bacteria genome.";
RL Submitted (MAY-2017) 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:ORT49622.1}.
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DR EMBL; JXQD01000025; ORT49622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1MQE1; -.
DR STRING; 1603038.ST37_14760; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000193432; 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 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; IPR031704; Glyco_hydro_36_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 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:UP000193432}.
FT DOMAIN 21..243
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
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 700 AA; 80057 MW; C3EB30B6753AA651 CRC64;
MTKFLHLQSK NHSLIIKTDK VPEILHWGAK IAHIDEDLLL STERPISQAR LDVDVPLSLC
PELGSGHFNA PGIEGHRDGY DWAPVFQLCS TKIENNHATF VMNDEVAQLE LTVEIKLDHA
TDVVQKRVTV RNTGNSNYYL GKLSSTLPLP THANELMTFH GRWCHEFQTQ RQRFEHGGFI
QENRRGRTSH ENFPGLFVGS NGFSEQLGQV WGFHLGWSGN HQMRADVRSD GRRFVQAGEL
LLSGESILDV DTQYQTPWLY GCYSQTGLNG ISQRFQQFVR DNIVSFPVKK PRPVHLNTWE
GIYFDHKPEY IKKMASEAAE MGVERFIIDD GWFIGRDGER AALGDWYLDE QKYPNGLEPV
IEHVNQQGME FGLWVEPEMV SEDSNLYRNH PDWVLGLKGY HQPSGRWQYV LDLQNPDCFN
YLFERLNDLL TRYNITYLKW DMNRELVQPG HQGRPAVHGQ THALYRLVDA LNHAHNNVEI
ESCSSGGGRI DFEILKRTQR FWASDCNDAL ERQAIQKGMS YFFPPEVMGA HIGPAECHST
NRRHGINMRG VTALSGHMGV ELDPVKESTQ EKAAFSRYIA LHKQYRHLLH GGRSFRIDPA
DKNQNIYGVE SDNEMLITVC QLAMLDHALP SPLRISCADI NAKYQVKLVE MPQTSFQLMK
QRPKWLDKTL TLSGDNLKEI GLTLPILDPE SALMVHLQKL
//
