ID   GANB_BACSU              Reviewed;         429 AA.
AC   O07013; O32260;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Endo-beta-1,4-galactanase {ECO:0000303|PubMed:27501980};
DE            Short=Galactanase {ECO:0000303|PubMed:27501980};
DE            EC=3.2.1.- {ECO:0000269|PubMed:27501980};
DE   AltName: Full=Arabinogalactan endo-beta-1,4-galactanase {ECO:0000305};
DE            EC=3.2.1.89 {ECO:0000305|PubMed:17056685};
DE   Flags: Precursor;
GN   Name=ganB {ECO:0000303|PubMed:27501980};
GN   Synonyms=galA {ECO:0000303|PubMed:17056685}, yvfO;
GN   OrderedLocusNames=BSU34120;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9287030; DOI=10.1128/jb.179.17.5636-5638.1997;
RA   Daniel R.A., Haiech J., Denizot F., Errington J.;
RT   "Isolation and characterization of the lacA gene encoding beta-
RT   galactosidase in Bacillus subtilis and a regulator gene, lacR.";
RL   J. Bacteriol. 179:5636-5638(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Denizot F.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   FUNCTION IN GALACTAN DEGRADATION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=17056685; DOI=10.1128/aem.01306-06;
RA   Shipkowski S., Brenchley J.E.;
RT   "Bioinformatic, genetic, and biochemical evidence that some glycoside
RT   hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer
RT   hydrolases.";
RL   Appl. Environ. Microbiol. 72:7730-7738(2006).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX   PubMed=27501980; DOI=10.1128/jb.00468-16;
RA   Watzlawick H., Morabbi Heravi K., Altenbuchner J.;
RT   "Role of the ganSPQAB operon in degradation of galactan by Bacillus
RT   subtilis.";
RL   J. Bacteriol. 198:2887-2896(2016).
CC   -!- FUNCTION: Involved in galactan degradation (PubMed:17056685,
CC       PubMed:27501980). Degrades arabinose-free galactan to
CC       galactooligosaccharides, producing galactotetraose as the main product
CC       along with galactotriose, galactobiose, and galactose
CC       (PubMed:27501980). Is also able to degrade galactotetraose,
CC       galactotriose and galactobiose, suggesting an additional exo-mode of
CC       activity (PubMed:27501980). May hydrolyze the beta-1,4-galactan
CC       linkages of the galactan portion of arabinogalactan type I, a pectic
CC       plant polysaccharide from which most of the arabinose has been removed
CC       (Probable). {ECO:0000269|PubMed:17056685, ECO:0000269|PubMed:27501980,
CC       ECO:0000305|PubMed:17056685}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic
CC         linkages in type I arabinogalactans.; EC=3.2.1.89;
CC         Evidence={ECO:0000305|PubMed:17056685};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q65CX5};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q65CX5};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5 with AZCL galactan as substrate.
CC         {ECO:0000269|PubMed:27501980};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius with AZCL galactan as
CC         substrate. {ECO:0000269|PubMed:27501980};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17056685}.
CC   -!- INDUCTION: Repressed by the transcriptional regulator GanR and induced
CC       by galactobiose. Also repressed by glucose.
CC       {ECO:0000269|PubMed:27501980}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family. {ECO:0000305}.
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DR   EMBL; Z94043; CAB08009.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15417.2; -; Genomic_DNA.
DR   PIR; F70038; F70038.
DR   RefSeq; NP_391292.2; NC_000964.3.
DR   RefSeq; WP_003243128.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O07013; -.
DR   SMR; O07013; -.
DR   STRING; 224308.BSU34120; -.
DR   CAZy; GH53; Glycoside Hydrolase Family 53.
DR   PaxDb; 224308-BSU34120; -.
DR   EnsemblBacteria; CAB15417; CAB15417; BSU_34120.
DR   GeneID; 937086; -.
DR   KEGG; bsu:BSU34120; -.
DR   PATRIC; fig|224308.179.peg.3699; -.
DR   eggNOG; COG3867; Bacteria.
DR   InParanoid; O07013; -.
DR   OrthoDB; 9768786at2; -.
DR   BioCyc; BSUB:BSU34120-MONOMER; -.
DR   BioCyc; MetaCyc:BSU34120-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031218; F:arabinogalactan endo-1,4-beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015926; F:glucosidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR011683; Glyco_hydro_53.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34983; ARABINOGALACTAN ENDO-BETA-1,4-GALACTANASE A; 1.
DR   PANTHER; PTHR34983:SF2; ENDO-BETA-1,4-GALACTANASE; 1.
DR   Pfam; PF07745; Glyco_hydro_53; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Glycosidase; Hydrolase; Metal-binding; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..429
FT                   /note="Endo-beta-1,4-galactanase"
FT                   /id="PRO_0000012222"
FT   ACT_SITE        194
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   ACT_SITE        292
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         146..149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         233..234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         301
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         303
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         305
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         307
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         396
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
FT   BINDING         399
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q65CX5"
SQ   SEQUENCE   429 AA;  47279 MW;  8A32869EA42127AD CRC64;
     MKSKVKMFFA AAIVWSACSS TGYAAAIEKE KHVSELRAED LFVKKVEGMN KDFIKGADVS
     SVIALENSGV TFYNTNGKRQ DIFTTLKQAG VNYVRVRIWN HPYDSNGNGY GGGNNDVQKA
     IEIGKRATAN GMKVLADFHY SDFWADPAKQ KVPKAWANLS FEAKKAKLYE YTKQSLQKMI
     KEGVDIGMVQ VGNETTGGFA GETDWTKMCQ LFNEGSRAVR ETNSNILVAL HFTNPETAGR
     YSFIAETLSK NKVDYDVFAS SYYPFWHGTL QNLTSVLKAV ANTYGKKVMV AETSYTYTAE
     DGDGHGNTAP KSGQTLPYPI SVQGQATAVR DVMEAVANTG KAGLGVFYWE PAWIPVGPKT
     QIEKNKVLWE TYGSGWASSY AAEYDPEDAG KWYGGSAVDN QALFDFNGHP LPSLQVFQYA
     ESGHIPKKR
//