ID   KOJP_CALS4              Reviewed;         771 AA.
AC   Q8RBL8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Kojibiose phosphorylase;
DE            EC=2.4.1.230;
GN   Name=kojP; OrderedLocusNames=TTE0798;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
CC   -!- FUNCTION: Hydrolyzes kojibiose in the presence of an inorganic
CC       phosphoric acid to form D-glucose and beta-D-glucose-1-phosphoric acid.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=kojibiose + phosphate = beta-D-glucose 1-phosphate + D-
CC         glucose; Xref=Rhea:RHEA:11176, ChEBI:CHEBI:4167, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57684, ChEBI:CHEBI:142460; EC=2.4.1.230;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR   EMBL; AE008691; AAM24055.1; -; Genomic_DNA.
DR   RefSeq; WP_011025193.1; NC_003869.1.
DR   AlphaFoldDB; Q8RBL8; -.
DR   SMR; Q8RBL8; -.
DR   STRING; 273068.TTE0798; -.
DR   CAZy; GH65; Glycoside Hydrolase Family 65.
DR   PRIDE; Q8RBL8; -.
DR   EnsemblBacteria; AAM24055; AAM24055; TTE0798.
DR   KEGG; tte:TTE0798; -.
DR   eggNOG; COG1554; Bacteria.
DR   HOGENOM; CLU_006285_2_1_9; -.
DR   OMA; FFIYVYP; -.
DR   OrthoDB; 179460at2; -.
DR   Proteomes; UP000000555; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0033831; F:kojibiose phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR   InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..771
FT                   /note="Kojibiose phosphorylase"
FT                   /id="PRO_0000108016"
FT   ACT_SITE        498
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         358..359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         611..612
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ   SEQUENCE   771 AA;  89640 MW;  A0922A5CDCF631F5 CRC64;
     MQVIKKVEEL MGDAKWLVFQ EEYNNKLNGK YETLFTLTNG YMGIRGTFEE GSEGERPGSF
     IAGIFNRGEA QVRELVNVQN WMRLKIYIEG EEIRLDRCEL LEFQRILDMK KGVLFRKTVV
     KDDKGRVTKI EGYRFVSRSN RHRSAIRFFI TPLNYEGVIG VENLIEGTVL NSATHPKYRV
     KHLKVVKNES ICKSGIYLET ATTDENKRIA VGSTLRIYNL EDINRENIAF FRRFIPLGEN
     SAEYLEFKGE REKTVVVDKF AVTYTSRDVE KDLLKNAVEN DLFDFVSRGF DEELEKHIAE
     YDKLWSVADI TIEGDEEADI ALRFNIFHLM SSVNEKDPWV SIGAKGLHGE GYKGHVFWDT
     EIFMLPFFIY VYPEAARTLL MYRYNMLDAA RRNAALNGYK GAQYPWESAD TGMEETPKWG
     FDYKGNPVRI WTGDLEHHIT ADVAFAVWEY FRATNDIDFM LNFGAEIILE TARFWASRCE
     YVEELDRYEI NNVIGPDEFH EHVNNNAYTN YFAKWNIKKG LEIIGELKEN YPDYYYAITH
     KISLTPEEVE KWKEVEKKIY IPYDKDKKLI EQFEGYFEKK DYVIEKFDEN NMPVWPEGVD
     VTKLGDTQLI KQADVVMLML LMPEEFDEET KRINYEYYEK RTMHKSSLSP SMYAIMGLKV
     GDHRNAYQSF IRSAKVDLAD NQGNAVEGIH AASCGGTWQV AVFGFGGLEI DREGVLNINP
     WLPEKWEKLS YKIFWKGSLL EVTVAKEEVS VKKLKGRETV KIKVKGKEMA L