ID A0A1B9AQM2_9BACI Unreviewed; 744 AA.
AC A0A1B9AQM2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=A8L44_07325 {ECO:0000313|EMBL:OCA86217.1};
OS Bacillus sp. FJAT-27986.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA86217.1, ECO:0000313|Proteomes:UP000092673};
RN [1] {ECO:0000313|EMBL:OCA86217.1, ECO:0000313|Proteomes:UP000092673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA86217.1,
RC ECO:0000313|Proteomes:UP000092673};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J.,
RA Liu B., Liu G.;
RT "Bacillus sp. FJAT-27986.";
RL Submitted (MAY-2016) 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:OCA86217.1}.
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DR EMBL; MAYV01000014; OCA86217.1; -; Genomic_DNA.
DR RefSeq; WP_066104576.1; NZ_MAYV01000014.1.
DR AlphaFoldDB; A0A1B9AQM2; -.
DR STRING; 1743146.A8L44_07325; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000092673; 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:UP000092673}.
FT DOMAIN 32..288
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 651..740
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 481
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 551
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 369..370
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 446
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 479..483
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 529
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 551
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 744 AA; 85706 MW; A405E33551B75E92 CRC64;
MNKLIKVNKN KLEFHLSNSK VSYLFRVMDQ INQLEHLYFG KSIRHQENFD FLMEREVRPS
NNQFEGDHTS SLEHIRQEYP GFGTSDFRYP AQQVRYPAGD RISRFEYADY RVMEGKPVLA
GLPATYTESP EEAETLEILL KDAYSELTLY IFYTIYKDRP VIARSAKFTN NGSEDYELET
AMSLSIDFSD DNFELIHLNG AWTRENHLER KPVITGVQSI SSTRGASSHA HNPFMALVLP
ETTEHAGEAY GFSLIYSGNF LAQIEVDTYK VTRAMMGINP FQFAWKLKQG ESFQTPEAVL
VYSDSGLNEM SQALHDLYRT RLARGVWRDK ERPILINNWE ATYFDFNEEK ILEIARSGAE
LGMELFVLDD GWFGQRNDDS SSLGDWFVNS AKLPNGMKGL SEKIHALGLK FGLWFEPEMV
CKDTKLFKEH PDWLIQVPGK RLSHGRNQFV LDFSRSEVVE NVYEQMDAIL SDCQIDYIKW
DMNRYISEAY SIALPADQQG EVWHRYILGV YSLYERLIAK YPDILFESCA GGGGRFDPGM
LYYAPQGWAS DDTDAVERLK IQYGTSFVYP LSSIGSHVSA VPNHQVGRTT SMEMRANVAF
FGTFGYELDI TLLSEEEKDQ IKKDITFFKQ HRALIQQGTF FRLLSPFTNN ETAWMVVSKD
QTEAIVGYYE VLSKPNRPYE RLKLKGLAED KMYQINGDGK RFGDDLMQIG LLFGENFTGK
ADEFWSREKT KDYNSKLFYL NSIN
//
