ID A4XGP2_CALS8 Unreviewed; 756 AA. AC A4XGP2; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 02-SEP-2026, entry version 94. DE SubName: Full=Kojibiose phosphorylase {ECO:0000313|EMBL:ABP66077.1}; DE EC=2.4.1.230 {ECO:0000313|EMBL:ABP66077.1}; GN OrderedLocusNames=Csac_0439 {ECO:0000313|EMBL:ABP66077.1}; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T OS 6331). OC Bacteria; Bacillati; Bacillota; Bacillota incertae sedis; OC Caldicellulosiruptorales; Caldicellulosiruptoraceae; Caldicellulosiruptor. OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP66077.1, ECO:0000313|Proteomes:UP000000256}; RN [1] {ECO:0000313|EMBL:ABP66077.1, ECO:0000313|Proteomes:UP000000256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331 RC {ECO:0000313|Proteomes:UP000000256}; RX PubMed=18776029; DOI=10.1128/AEM.00968-08; RA van de Werken H.J., Verhaart M.R., VanFossen A.L., Willquist K., RA Lewis D.L., Nichols J.D., Goorissen H.P., Mongodin E.F., Nelson K.E., RA van Niel E.W., Stams A.J., Ward D.E., de Vos W.M., van der Oost J., RA Kelly R.M., Kengen S.W.; RT "Hydrogenomics of the extremely thermophilic bacterium Caldicellulosiruptor RT saccharolyticus."; RL Appl. Environ. Microbiol. 74:6720-6729(2008). RN [2] {ECO:0007829|PDB:3WIQ, ECO:0007829|PDB:3WIR} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=24255995; DOI=10.1111/febs.12622; RA Okada S., Yamamoto T., Watanabe H., Nishimoto T., Chaen H., Fukuda S., RA Wakagi T., Fushinobu S.; RT "Structural and mutational analysis of substrate recognition in kojibiose RT phosphorylase."; RL FEBS J. 281:778-786(2014). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. CC {ECO:0000256|ARBA:ARBA00006768}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000679; ABP66077.1; -; Genomic_DNA. DR RefSeq; WP_011916030.1; NC_009437.1. DR PDB; 3WIQ; X-ray; 2.80 A; A=1-756. DR PDB; 3WIR; X-ray; 2.05 A; A/B/C/D=1-756. DR AlphaFoldDB; A4XGP2; -. DR SMR; A4XGP2; -. DR STRING; 351627.Csac_0439; -. DR CAZy; GH65; Glycoside Hydrolase Family 65. DR KEGG; csc:Csac_0439; -. DR eggNOG; COG1554; Bacteria. DR HOGENOM; CLU_006285_2_1_9; -. DR OrthoDB; 9758855at2; -. DR BRENDA; 2.4.1.230; 1055. DR EvolutionaryTrace; A4XGP2; -. DR Proteomes; UP000000256; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:TreeGrafter. 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; Glycoside hydrolase, family 65, N-terminal domain; 1. DR Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase_sf. DR InterPro; IPR012341; 6hp_glycosidase-like_sf. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR037018; GH65_N. DR InterPro; IPR005194; Glyco_hydro_65_C. DR InterPro; IPR005195; Glyco_hydro_65_M. DR InterPro; IPR005196; Glyco_hydro_65_N. DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase. DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1. DR PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1. 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; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1. DR PDBsum; 3WIQ; -. DR PDBsum; 3WIR; -. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3WIQ, ECO:0007829|PDB:3WIR}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000313|EMBL:ABP66077.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000256}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABP66077.1}. FT DOMAIN 16..288 FT /note="Glycoside hydrolase family 65 N-terminal" FT /evidence="ECO:0000259|Pfam:PF03636" FT DOMAIN 308..684 FT /note="Glycoside hydrolase family 65 central catalytic" FT /evidence="ECO:0000259|Pfam:PF03632" FT DOMAIN 697..754 FT /note="Glycoside hydrolase family 65 C-terminal" FT /evidence="ECO:0000259|Pfam:PF03633" FT ACT_SITE 483 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50" FT BINDING 343..344 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51" FT BINDING 596..597 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51" FT DISULFID 43 FT /evidence="ECO:0007829|PDB:3WIQ" FT DISULFID 43 FT /note="Interchain" FT /evidence="ECO:0007829|PDB:3WIR" SQ SEQUENCE 756 AA; 87601 MW; 9666D2B21B66B228 CRC64; MKLSEREWLI EQDKLEASGK FETCFALTNG YIGIRGINEE VFCEETPGTY IAGVFDKSTA QVTELVNLPN PIGLRIYINR EFLNPLKCEI LEFKRVLDLK QGILYRKLRL KDVKGRITTI EGFRFVSMNN KNLIVQKYDV VCENYSAVLN VESFIDATTV NSKDVPNDRV KHYEIDKKKD FADGIYLGIT TKDKKYKVGI ASSTKVLLNN QRCYFNRFTK DLGYIITENF EVEAKQGERY EIEKLTVLVS SREKNVGDVF ETCTNKLKEF ETKSAEKLLF EHIEEYKRLW DVANIDIVGD EVANKSVKFN IFHLISMANP EDEHVSLGAK GLHGEGYKGH VFWDTEIFML PFYIYTNPAA AKAMLMYRYN LLDAARENAR KNGYKGAQFP WESADTGEEE TPKWGYDYLG NPVRIWTGDI EYHISADIAY AVMNYVRATD DIDFLLNYGS EIIIETARFW ASICKYNKEK GRYEINDVIG PDEFHEHCNN NAYTNYLAKW NLLKASELCN LLLEKYPKYF EKLSKKINLS DEEPFVWQEI ASKIYIPYHP DKKLIEQFEG YFNLKDFVIK EYDQNNMPVW PEGVELDKLN NYQLIKQADV VMLLYLLGEE FDDQTKKINY DYYEKRTMHK SSLSPSIYAL MGVRVGETNR AYINFMRTAL TDLEDNQGNT HLGIHAASLG GTWQALVFGF GGISIEKDDV LSVNPWLPEK WESLKFSIWW KGNLLDFKIT KDNVEVKKRV EKGNVKLKIK GQEAII //