ID   Q65LL3_BACLD            Unreviewed;       432 AA.
AC   Q65LL3; Q62X04;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 127.
DE   SubName: Full=Alpha-D-galactoside galactohydrolase, Glycoside Hydrolase Family 4,MelA {ECO:0000313|EMBL:AAU22704.1};
GN   Name=melA {ECO:0000313|EMBL:AAU22704.1};
GN   OrderedLocusNames=BL01356 {ECO:0000313|EMBL:AAU22704.1};
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU22704.1, ECO:0000313|Proteomes:UP000000606};
RN   [1] {ECO:0000313|EMBL:AAU22704.1, ECO:0000313|Proteomes:UP000000606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC   9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC   {ECO:0000313|Proteomes:UP000000606};
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU361152};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC       {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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DR   EMBL; CP000002; AAU22704.1; -; Genomic_DNA.
DR   RefSeq; WP_003180406.1; NC_006270.3.
DR   AlphaFoldDB; Q65LL3; -.
DR   STRING; 279010.BL01356; -.
DR   GeneID; 92862275; -.
DR   KEGG; bld:BLi01143; -.
DR   KEGG; bli:BL01356; -.
DR   PATRIC; fig|279010.13.peg.1126; -.
DR   eggNOG; COG1486; Bacteria.
DR   HOGENOM; CLU_045951_1_1_9; -.
DR   Proteomes; UP000000606; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR   Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR   InterPro; IPR053715; GH4_Enzyme_sf.
DR   InterPro; IPR019802; GlycHydrolase_4_CS.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF011657; PRK15076.1; 1.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW   Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR601088-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000606}.
FT   DOMAIN          194..404
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            110
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   432 AA;  48975 MW;  5B5642BDA979DA88 CRC64;
     MTKIAFIGAG STIFAKNVLG DCLMVPAVNG FEFALYDIDP KRLKESKDML EHLKNRYNDT
     VSIRAYDDRK EALAGAKYVI NAIQVGGYKP GTVIDFEIPK KYGLKQTIAD TVGIGGIFRA
     LRTIPVLLDM AKDIESAAPD AWLLNYTNPM ASLTGALLRY TDVKTVGLCH SVQVCTKDLF
     KSLGMKHERI EEKIAGINHM AWLLEVKQDG RDLYPEIKKR AKEKQKTKHG DMVRFELMDK
     FGYYVTESSE HNAEYHPYFI KSRYPELIEE LNIPIDEYLR RCEKQIQNWE KMRGEIVGNR
     HLTHERSNEY GSRIIEAMET GQPFTFGGNV LNKGLITNLP EKAVVEVTCV AERNRITPCY
     AGELPEQLAA LNRTNINTQL LTIEAATTKR KEHIYHAALL DPHTAAELSM DDIVSMCDEL
     IEAHGDWLPE FE
//