ID   KOJP_THEBR              Reviewed;         775 AA.
AC   Q8L163;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Kojibiose phosphorylase;
DE            EC=2.4.1.230;
GN   Name=kojP;
OS   Thermoanaerobacter brockii (Thermoanaerobium brockii).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=29323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 35047 / HTRI;
RA   Kubota M., Toshio M., Hiroto C., Tomoyoki N.;
RT   "DNA encoding kojibiose phosphorylase obtainable from thermoanaerobium,
RT   it's preparation and uses.";
RL   Patent number US6140487, 31-OCT-2000.
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       Can act with alpha-1,2-oligoglucans, such as selaginose, as substrate,
CC       but more slowly. Inactive when disaccharides with linkages other than
CC       alpha-1,2 linkages, such as sophorose, trehalose, neotrehalose,
CC       nigerose, laminaribiose, maltose, cellobiose, isomaltose, gentiobiose,
CC       sucrose and lactose, are used as substrates.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5.;
CC       Temperature dependence:
CC         Optimum temperature is about 65 degrees Celsius.;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR   EMBL; AB073931; BAB97300.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8L163; -.
DR   SMR; Q8L163; -.
DR   CAZy; GH65; Glycoside Hydrolase Family 65.
DR   BioCyc; MetaCyc:MON-18543; -.
DR   BRENDA; 2.4.1.230; 1463.
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   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..775
FT                   /note="Kojibiose phosphorylase"
FT                   /id="PRO_0000108015"
FT   ACT_SITE        501
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         361..362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         614..615
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ   SEQUENCE   775 AA;  89700 MW;  FB9760F02B220E56 CRC64;
     MVKHMFLEDV NNLISDDKWL IFQNEYNTEV NPRYETLFTL TNGYMGVRGT FEEGSEGERS
     GNFIAGIFDK SDAQVREIVN AQNWLRIKLY VEGEELSLDK CQLIEFKRIL DMKKGILFRS
     MLIKDSKDRI TRIEGYRFIS RSDLHRSAIK LFVTPVNYSG VVGIESIIDG TVLNSADSPK
     HRVKHLKVAD NSSLNKSGVY LETATIDDDI RIATGSAVRL YHYEDKEKNN IAKFKRFLPL
     GEMSIEYFEF DGTENKTVVI DKFIITYTSR DVKKGLLKST VEKELFAFAG EGIDKELQRH
     IEVYEELWSV ADINIEGDEE ADKALRFNIF HLMSSVNEND PMVSIAAKAL HGEGYKGHVF
     WDTEIFMLPF FIYVHPKAAK TLLMYRYNML DAARKNAALN GYKGAQYPWE SADTGEEETP
     KWGFDYMGNP VRIWTGDLEH HITADIAFAV WEYFRATEDI EFMLNYGAEV IFETARFWVS
     RCEYVKELDR YEINNVIGPD EFHEHVDNNA YTDYLAKWNI KKGLELINML KEKYPEHYHA
     ISNKKCLTNE EMEKWKEVEE KIYIPYDKDK KLIEQFEGYF DKKDYVIDKF DENNMPIWPE
     GVDITKLGDT QLIKQADVVM LMLLLGEEFD EETKRINYEY YEKRTMHKSS LGPSMYAIMG
     LKVGDHKNAY QSFMRSANVD LVDNQGNTKE GLHAASAGGT WQVVVFGFGG MEIDKEGALN
     INSWLPEKWD KLSYKVFWKG NLIEVIVTKQ EVTVKKLKGK GNIKVKVKGK ELTIE