CBPA_THENN
ID CBPA_THENN Reviewed; 813 AA.
AC B9K7M6; O52504;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Cellobiose phosphorylase {ECO:0000303|PubMed:10960102};
DE EC=2.4.1.20 {ECO:0000269|PubMed:10960102};
GN Name=cbpA {ECO:0000303|PubMed:10960102}; OrderedLocusNames=CTN_0783;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RX PubMed=10960102; DOI=10.1128/jb.182.18.5172-5179.2000;
RA Yernool D.A., McCarthy J.K., Eveleigh D.E., Bok J.-D.;
RT "Cloning and characterization of the glucooligosaccharide catabolic pathway
RT beta-glucan glucohydrolase and cellobiose phosphorylase in the marine
RT hyperthermophile Thermotoga neapolitana.";
RL J. Bacteriol. 182:5172-5179(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorolysis of cellobiose, yielding glucose
CC 1-phosphate and glucose. Is inactive against cellotriose and the
CC disaccharides lactose, chitobiose and xylobiose. May be the primary
CC enzyme for processing cellobiose in T.neapolitana.
CC {ECO:0000269|PubMed:10960102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellobiose + phosphate = alpha-D-glucose 1-phosphate + D-
CC glucose; Xref=Rhea:RHEA:19493, ChEBI:CHEBI:4167, ChEBI:CHEBI:17057,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.20;
CC Evidence={ECO:0000269|PubMed:10960102};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.42 mM for cellobiose {ECO:0000269|PubMed:10960102};
CC Note=kcat is 26.3 sec(-1). {ECO:0000269|PubMed:10960102};
CC pH dependence:
CC Optimum pH is 4.5 to 6.0. {ECO:0000269|PubMed:10960102};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:10960102};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000303|PubMed:10960102}.
CC -!- PATHWAY: Glycan metabolism; beta-D-glucan degradation.
CC {ECO:0000303|PubMed:10960102}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 94 family. {ECO:0000305}.
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DR EMBL; AF039487; AAB95491.2; -; Genomic_DNA.
DR EMBL; CP000916; ACM22959.1; -; Genomic_DNA.
DR RefSeq; WP_015919276.1; NC_011978.1.
DR AlphaFoldDB; B9K7M6; -.
DR SMR; B9K7M6; -.
DR STRING; 309803.CTN_0783; -.
DR CAZy; GH94; Glycoside Hydrolase Family 94.
DR EnsemblBacteria; ACM22959; ACM22959; CTN_0783.
DR KEGG; tna:CTN_0783; -.
DR eggNOG; COG3459; Bacteria.
DR HOGENOM; CLU_019054_0_0_0; -.
DR OMA; YVYAQMI; -.
DR BRENDA; 2.4.1.20; 6332.
DR SABIO-RK; B9K7M6; -.
DR UniPathway; UPA00350; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000000445; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0047738; F:cellobiose phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd11754; GH94N_CBP_like; 1.
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; IPR009342; Carb-bd_put_dom.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR033432; GH36_catalytic.
DR InterPro; IPR037825; GH94N_CBP.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR010383; Glyco_hydrolase_94.
DR Pfam; PF17167; Glyco_hydro_36; 1.
DR Pfam; PF06165; Glyco_transf_36; 1.
DR SMART; SM01068; CBM_X; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Glycosyltransferase;
KW Polysaccharide degradation; Transferase.
FT CHAIN 1..813
FT /note="Cellobiose phosphorylase"
FT /id="PRO_0000431443"
FT ACT_SITE 481
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CONFLICT 182
FT /note="Y -> F (in Ref. 1; AAB95491)"
FT CONFLICT 197
FT /note="Y -> F (in Ref. 1; AAB95491)"
FT CONFLICT 328
FT /note="Missing (in Ref. 1; AAB95491)"
SQ SEQUENCE 813 AA; 93679 MW; 0D6AE176E4C0D659 CRC64;
MKFGYFDDKN REYVIVTPRT PYPWINYLGT EDFFSIISHM AGGYCFYKDA RLRRITRFRY
NNVPTDAGGR YFYIREEDGD FWSPTWMPVR RDLSFFEARH GLGYTKIAGE RNGLRATITF
FVPRHFTGEV HHLVLQNRTE RPRRIKLFSF IEFCLWNALD DMTNFQRNYS TGEVEIEGSV
IYHKTEYRER RNHYAFYSVN HSIDGFDTDR ESFMGLYNGF EAPQAVVEGN PRNSVASGWA
PIASHYLELE IPPLGEKELI FILGYVENPE EEKWERPGVI NKKRAKEMIE RFKTGEDVER
ALKELKEYWD ELLGRIQVET HDEKLNRMVN IWNQYQCMVT FNIARSASYF ESGISRGIGF
RDSNQDILGF VHMIPEKARQ RILDLASIQF EDGSTYHQFQ PLTKKGNNEI GGGFNDDPLW
LILSTSAYIK ETGDWSILNE EVPFDNDPDK KATLFEHLKR SFYFTVNNLG PHGLPLIGRA
DWNDCLNLNC FSKNPDESFQ TTVNALDGRV AESVFIAGLF VLAGKEFVEI CRRLGLEDEA
KEAEKHVKKM IETTLEYGWD GEWFLRAYDA FGRKVGSKEC EEGKIFIEPQ GMCVMAGIGV
ENGYAKKALD SVKEHLDTPY GLVLQQPAYS RYYIELGEIS SYPPGYKENA GIFCHNNPWV
AIAETVIGRG DRAFEIYRKI TPAYLEDISE IHRTEPYVYA QMVAGKDAPR HGEAKNSWLT
GTAAWSFVAI TQYILGVRPT YDGLMVDPCI PEDWDGFKIT RRFRGATYEI TVKNPHHVSK
GVKEIIVDGK KIEGQVLPVF NDGKVHRVEV LMG
