GANB_BACSU
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 03-AUG-2022, entry version 128.
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; Firmicutes; 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; O07013; -.
DR PRIDE; O07013; -.
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 OMA; GVNTVRQ; -.
DR BioCyc; BSUB:BSU34120-MON; -.
DR BioCyc; MetaCyc:BSU34120-MON; -.
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 InterPro; IPR011683; Glyco_hydro_53.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34983; PTHR34983; 1.
DR Pfam; PF07745; Glyco_hydro_53; 1.
DR SUPFAM; SSF51445; SSF51445; 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
