ID N1MIP9_9SPHN Unreviewed; 733 AA.
AC N1MIP9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=EBBID32_9820 {ECO:0000313|EMBL:CCW16644.1};
OS Sphingobium indicum BiD32.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW16644.1, ECO:0000313|Proteomes:UP000013201};
RN [1] {ECO:0000313|EMBL:CCW16644.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW16644.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Le V.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW16644.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW16644.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Nielsen J.L., Zhou N.A., Kjeldal H.;
RT "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL Submitted (APR-2013) 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:CCW16644.1}.
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; CAVK010000049; CCW16644.1; -; Genomic_DNA.
DR AlphaFoldDB; N1MIP9; -.
DR Proteomes; UP000013201; 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:UP000013201};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..733
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004108082"
FT DOMAIN 49..280
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 645..728
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 473
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 543
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
SQ SEQUENCE 733 AA; 80244 MW; EF4B6AEA03DD4171 CRC64;
MRSLAALTAI LCLTLPATLL AKVSASADGK LLRLDGGGVT YAMGVDEKGY LQPLYWGAAL
DAAAPLVAKA PGELSGFDPA GSITPQEYAG QGEGLVSEPG VKAVFADGNR DLVLKYRRHS
VSGETLTVEL ADISRALTVT LRYTIDPDTG VIARSASLRN GDVRPVRIDQ IAAATFTLPV
GDDYRLHYLT GRHGAEWSQV DTPVTPALTV LESRRGSTGH GNQPWFAIGK DGQTSETDGP
VWYGALAWSG SFRLSVGADN LGRVRISGGY NPYDFSWSLK PGETLETPVF YAGYAAKGMG
DASRRFHAFQ RASIIPGGAK AKIRPVLYNS WEATTFNVTE AGQMALAEKA AKLGVERFVV
DDGWFGARND DKAGLGDWTV NRTKFPNGLK PLIDKVKSLG MDFGLWVEPE MVNPDSDLYR
AHPDWVLAFP GRPRTEGRNQ LLLNLARTDV RDHLLNWLDR LVRDNDIAFL KWDYNRNWTE
AGWPQMPVQD QQRVQVAYVR NLYHILAELR RRHPGLEIEG CSGGGGRIDL GIMALTDQSW
TSDNTDPFDR LTIQDGFTQA YAPSIMMAWV TDSPNWANGR QTSLDYRFLS AMQGSLGLGA
NLDHWQQADF ATATKWIAAY KDIRATVQRG DLYRIAPPRA GAATSATVYV APDKKQAVLF
QMLHSSMFRD NVEALRVQGL DPARRYAVRM LGGAALPDGV PGHASGAYWM EQGVRMKLKG
DFQGAALVFE VMP
//
