ID A0A0Q7JDT3_9BACL Unreviewed; 736 AA.
AC A0A0Q7JDT3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=ASD40_07190 {ECO:0000313|EMBL:KQX51856.1};
OS Paenibacillus sp. Root444D2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736538 {ECO:0000313|EMBL:KQX51856.1, ECO:0000313|Proteomes:UP000051657};
RN [1] {ECO:0000313|EMBL:KQX51856.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX51856.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX51856.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX51856.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 36 family.
CC {ECO:0000256|ARBA:ARBA00006202}.
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:KQX51856.1}.
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DR EMBL; LMEO01000034; KQX51856.1; -; Genomic_DNA.
DR RefSeq; WP_057304903.1; NZ_LMEO01000034.1.
DR AlphaFoldDB; A0A0Q7JDT3; -.
DR STRING; 1736538.ASD40_07190; -.
DR Proteomes; UP000051657; 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:UP000051657}.
FT DOMAIN 30..286
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 650..732
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 479
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 549
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 367..368
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 477..481
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 736 AA; 83569 MW; C94B28C1350D700B CRC64;
MGIVYDSNSQ TFHLQGKSSS YIMQLIKSKY LAHVHWGRQI RGTNPGNLLA IRRRCSFSPS
TDPNDLTLSL DTLPQEFPAY GGSDFRVPAY QVQLEDGTTV SELIYESHRI YAGKAPLEGL
PSTYTENDCE AESIDIVLVD PTIGLKAILT YTVFLDCDAI TRSVRFMNVG NQSIKLLRAL
SFGIDISHCD FDMLHLSGTW ARERHIERRP ILTGGSVIES RRGSSSHSLN PFMALLSKQA
DEDHGEAYGF SLVYSGSFVA QAEVDPYGTT RVVMGINSFD FSWLLEPGQT FQTPEAVLVY
SAEGIGGMSR TYHRLYRTRL CRGQFRDRHR PILINNWEAT YFNFNADKIE ELARVGKELG
LELLVLDDGW FGKRDNDKSS LGDWFVDRGK LPQGMPDLVS RVKQQDLEFG LWFEPEMVSP
DSDLYRAHPD WCLHIPGRRR TEARQQLILD YSRQDVRDYI VTVITDILAS SPITYVKWDM
NRNMTEIGSA QLPPERQRET AHRYMLGLYE VMERITSAFP SVLFESCSGG GGRFDPGMLY
YMPQTWTSDN TDAVERLKIQ YGTSIVYPIS TMGAHVSAVP NHQVHRTTPL DMRGNVAMSG
NFGYELDLTA FTEAEKETVK KQVALYKQLR PLIQFGEFYR LISPFEHISA AWMFVSEDKK
EALVAFFQVL SEPNAPLRKL RLKGLAAESN YLLYDAEDQG NGVEIFGGDE LMHVGLNLPI
WKGDFRSRLY RLKMEE
//
