ID A0A494X1H2_9BURK Unreviewed; 713 AA.
AC A0A494X1H2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=D7S89_23480 {ECO:0000313|EMBL:RKP44170.1};
OS Trinickia fusca.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=2419777 {ECO:0000313|EMBL:RKP44170.1, ECO:0000313|Proteomes:UP000280434};
RN [1] {ECO:0000313|EMBL:RKP44170.1, ECO:0000313|Proteomes:UP000280434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7MK8-2 {ECO:0000313|EMBL:RKP44170.1,
RC ECO:0000313|Proteomes:UP000280434};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. 7MK8-2, isolated from soil.";
RL Submitted (OCT-2018) 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:RKP44170.1}.
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DR EMBL; RBZV01000014; RKP44170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494X1H2; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000280434; 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:UP000280434}.
FT DOMAIN 28..248
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 616..700
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 451
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 515
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 339..340
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 449..453
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 493
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 713 AA; 79442 MW; 1F677E42103BD4AC CRC64;
MSETSLIHVD GTTVSLVFER TAGMPPAWRH FGARRHDVEH AWPIAGVRPH PPTLLDGDPV
LTVLPTHGFG WFQQPALAGG RPAGHGDLDW AHAFCLEDVC WEPHAIVFKL ADKTAMLGLT
ISYAIDPESD VVSAWAELEN RGDVPFRVDW LAAACVPLPA DMDQVLGFTG RWTLEFQEAR
ERLGVATWRR DNRRGRTSND SFPGVIVGTA LDDDTGAVLG AHLGWSGNHT ILIEPLNDGR
RQLQIGEWLA PGEVVLGYGE RYRTPTAYLS FGTDGLNGLA SHFHRFVRKR LLAWPHGRMK
ARPVHLNTWE AVYCNHDLDD LKSLADAAAR LGIERFVLDD GWFHRRDHDR AGLGDWWPDA
RHYPHGLVPL VDHVQRLGMQ FGLWVEPEMV NPDSDLYRAH PDWVLRLDGR PVVTGRHQLV
LDLANAAVTD YLFDSLARLL SEQPIAYLKW DMNRDLAAAG HGGRAAYRRQ TLAFYRLIGR
VREAFPTVEI ESCASGGSRA DYGVLAHTHR IWTSDCNDAL TRIDIQRGFL RFFPPEVMGA
HIGPFHSHTT HRCHALAFRA AVALFGHLGI EMDVRTLPTE EAAELAYWIA VFKQWRHVVH
EGVLRQGNLG DSLAWVQATS ADGSASLVAV YRKREDTARY MPALPLKGLL DERRYLVRVL
HQPAAPHFVK KTDLLTSLAG DGVVLTGATL RESGIPLPPM PPESATVISC RAV
//
