GANB_BACLD
ID GANB_BACLD Reviewed; 424 AA.
AC Q65CX5; Q62NF0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Endo-beta-1,4-galactanase {ECO:0000303|PubMed:15312766};
DE Short=Galactanase {ECO:0000305};
DE EC=3.2.1.- {ECO:0000269|PubMed:15312766};
DE AltName: Full=Arabinogalactan endo-beta-1,4-galactanase {ECO:0000250|UniProtKB:O07013};
DE EC=3.2.1.89 {ECO:0000250|UniProtKB:O07013};
DE AltName: Full=BLGAL {ECO:0000303|PubMed:15312766};
DE Flags: Precursor;
GN Name=ganB; Synonyms=galA, yvfO; OrderedLocusNames=BLi04276, BL00263;
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
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., Joergensen 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).
RN [3] {ECO:0007744|PDB:1R8L, ECO:0007744|PDB:1UR0, ECO:0007744|PDB:1UR4}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 28-424 IN COMPLEXES WITH CALCIUM
RP IONS; GALACTOBIOSE AND GALACTOTRIOSE, FUNCTION, AND COFACTOR.
RX PubMed=15312766; DOI=10.1016/j.jmb.2004.05.017;
RA Ryttersgaard C., Le Nours J., Lo Leggio L., Joergensen C.T.,
RA Christensen L.L., Bjoernvad M., Larsen S.;
RT "The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in
RT complex with two oligosaccharide products.";
RL J. Mol. Biol. 341:107-117(2004).
CC -!- FUNCTION: Involved in galactan degradation (PubMed:15312766). Degrades
CC arabinose-free galactan to galactooligosaccharides, producing
CC galactotetraose as the main product along with galactotriose,
CC galactobiose, and galactose (PubMed:15312766). May hydrolyze the beta-
CC 1,4-galactan linkages of the galactan portion of arabinogalactan type
CC I, a pectic plant polysaccharide from which most of the arabinose has
CC been removed (By similarity). {ECO:0000250|UniProtKB:O07013,
CC ECO:0000269|PubMed:15312766}.
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:0000250|UniProtKB:O07013};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15312766};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:15312766};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU25711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017333; AAU43089.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU25711.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011201775.1; NC_006270.3.
DR PDB; 1R8L; X-ray; 2.60 A; A/B=26-424.
DR PDB; 1UR0; X-ray; 2.50 A; A/B=26-424.
DR PDB; 1UR4; X-ray; 2.20 A; A/B=26-424.
DR PDB; 2CCR; X-ray; 2.30 A; A/B=26-424.
DR PDB; 2GFT; X-ray; 2.30 A; A/B=26-424.
DR PDB; 2J74; X-ray; 2.60 A; A/B=28-424.
DR PDBsum; 1R8L; -.
DR PDBsum; 1UR0; -.
DR PDBsum; 1UR4; -.
DR PDBsum; 2CCR; -.
DR PDBsum; 2GFT; -.
DR PDBsum; 2J74; -.
DR AlphaFoldDB; Q65CX5; -.
DR SMR; Q65CX5; -.
DR STRING; 279010.BL00263; -.
DR DrugBank; DB04248; beta-(1->4)-galactotriose.
DR DrugBank; DB02743; beta-D-galactopyranosyl-(1->4)-beta-D-galactopyranose.
DR DrugBank; DB02327; Triethylene glycol.
DR CAZy; GH53; Glycoside Hydrolase Family 53.
DR PRIDE; Q65CX5; -.
DR EnsemblBacteria; AAU25711; AAU25711; BL00263.
DR KEGG; bld:BLi04276; -.
DR KEGG; bli:BL00263; -.
DR PATRIC; fig|279010.13.peg.4362; -.
DR eggNOG; COG3867; Bacteria.
DR HOGENOM; CLU_011259_2_0_9; -.
DR OMA; GVNTVRQ; -.
DR OrthoDB; 1622507at2; -.
DR BioCyc; BLIC279010:BLI_RS21035-MON; -.
DR BRENDA; 3.2.1.89; 669.
DR EvolutionaryTrace; Q65CX5; -.
DR Proteomes; UP000000606; Chromosome.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..424
FT /note="Endo-beta-1,4-galactanase"
FT /id="PRO_0000371562"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT ACT_SITE 288
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT BINDING 142..145
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15312766"
FT BINDING 229..230
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15312766"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15312766"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15312766"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15312766,
FT ECO:0007744|PDB:1R8L, ECO:0007744|PDB:1UR0,
FT ECO:0007744|PDB:1UR4"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15312766,
FT ECO:0007744|PDB:1UR0, ECO:0007744|PDB:1UR4"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15312766,
FT ECO:0007744|PDB:1R8L, ECO:0007744|PDB:1UR0,
FT ECO:0007744|PDB:1UR4"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15312766,
FT ECO:0007744|PDB:1R8L, ECO:0007744|PDB:1UR0,
FT ECO:0007744|PDB:1UR4"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15312766"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15312766"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15312766,
FT ECO:0007744|PDB:1R8L, ECO:0007744|PDB:1UR0,
FT ECO:0007744|PDB:1UR4"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15312766,
FT ECO:0007744|PDB:1R8L, ECO:0007744|PDB:1UR0,
FT ECO:0007744|PDB:1UR4"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2GFT"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 157..177
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:1UR4"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 266..280
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 318..333
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:1UR4"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:1UR4"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:1UR4"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1UR0"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:1UR4"
FT HELIX 412..418
FT /evidence="ECO:0007829|PDB:1UR4"
SQ SEQUENCE 424 AA; 46225 MW; E6CC3D0D1B80D166 CRC64;
MKNVLAVFVV LIFVLGAFGT SGPAEAARDS GTAKSGLYVE KVSGLRKDFI KGVDVSSIIA
LEESGVAFYN ESGKKQDIFK TLKEAGVNYV RVRIWNDPYD ANGNGYGGGN NDLEKAIQIG
KRATANGMKL LADFHYSDFW ADPAKQKAPK AWANLNFEDK KTALYQYTKQ SLKAMKAAGI
DIGMVQVGNE TNGGLAGETD WAKMSQLFNA GSQAVRETDS NILVALHFTN PETSGRYAWI
AETLHRHHVD YDVFASSYYP FWHGTLKNLT SVLTSVADTY GKKVMVAETS YTYTAEDGDG
HGNTAPKNGQ TLNNPVTVQG QANAVRDVIQ AVSDVGEAGI GVFYWEPAWI PVGPAHRLEK
NKALWETYGS GWATSYAAEY DPEDAGKWFG GSAVDNQALF DFKGRPLPSL HVFQYVDTGT
PFKN
