ID   GANA_CELJU              Reviewed;         376 AA.
AC   P48841; B3PIY6;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Arabinogalactan endo-beta-1,4-galactanase;
DE            EC=3.2.1.89;
DE   AltName: Full=Endo-1,4-beta-galactanase;
DE            Short=Galactanase;
DE   Flags: Precursor;
GN   Name=ganB; Synonyms=gal53A-2, galA, ganA; OrderedLocusNames=CJA_0497;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], REACTION MECHANISM, INDUCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLU-161 AND GLU-270.
RX   PubMed=9398278; DOI=10.1021/bi9712394;
RA   Braithwaite K.L., Barna T., Spurway T.D., Charnock S.J., Black G.W.,
RA   Hughes N., Lakey J.H., Virden R., Hazlewood G.P., Henrissat B.,
RA   Gilbert H.J.;
RT   "Evidence that galactanase A from Pseudomonas fluorescens subspecies
RT   cellulosa is a retaining family 53 glycosyl hydrolase in which E161 and
RT   E270 are the catalytic residues.";
RL   Biochemistry 36:15489-15500(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.3 mM for 2,4-dinitrophenyl-beta-galactobioside (at pH 7 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:9398278};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:9398278};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:9398278};
CC   -!- INDUCTION: By galactan. {ECO:0000269|PubMed:9398278}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family. {ECO:0000305}.
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DR   EMBL; X91885; CAA62990.1; -; Genomic_DNA.
DR   EMBL; CP000934; ACE83887.1; -; Genomic_DNA.
DR   RefSeq; WP_012486177.1; NC_010995.1.
DR   AlphaFoldDB; P48841; -.
DR   SMR; P48841; -.
DR   STRING; 498211.CJA_0497; -.
DR   CAZy; GH53; Glycoside Hydrolase Family 53.
DR   PRIDE; P48841; -.
DR   EnsemblBacteria; ACE83887; ACE83887; CJA_0497.
DR   KEGG; cja:CJA_0497; -.
DR   eggNOG; COG3867; Bacteria.
DR   HOGENOM; CLU_011259_2_1_6; -.
DR   OMA; GVNTVRQ; -.
DR   OrthoDB; 1622507at2; -.
DR   Proteomes; UP000001036; 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   Calcium; Glycosidase; Hydrolase; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..376
FT                   /note="Arabinogalactan endo-beta-1,4-galactanase"
FT                   /id="PRO_0000012220"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT   ACT_SITE        270
FT                   /note="Nucleophile"
FT   BINDING         281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         161
FT                   /note="E->A: Partial loss of activity."
FT                   /evidence="ECO:0000269|PubMed:9398278"
FT   MUTAGEN         270
FT                   /note="E->A: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:9398278"
SQ   SEQUENCE   376 AA;  42315 MW;  BEC4F7243C6CAE10 CRC64;
     MKKKILAATA ILLAAIANTG VADNTPFYVG ADLSYVNEME SCGATYRDQG KKVDPFQLFA
     DKGADLVRVR LWHNATWTKY SDLKDVSKTL KRAKNAGMKT LLDFHYSDTW TDPEKQFIPK
     AWAHITDTKE LAKALYDYTT DTLASLDQQQ LLPNLVQVGN ETNIEILQAE DTLVHGIPNW
     QRNATLLNSG VNAVRDYSKK TGKPIQVVLH IAQPENALWW FKQAKENGVI DYDVIGLSYY
     PQWSEYSLPQ LPDAIAELQN TYHKPVMIVE TAYPWTLHNF DQAGNVLGEK AVQPEFPASP
     RGQLTYLLTL TQLVKSAGGM GVIYWEPAWV STRCRTLWGK GSHWENASFF DATRKNNALP
     AFLFFKADYQ ASAQAE