ID   CELAP_XANCP             Reviewed;         798 AA.
AC   Q8P3J4;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Cellobionic acid phosphorylase;
DE            EC=2.4.1.321;
DE   AltName: Full=4-O-beta-D-glucopyranosyl-D-gluconate:phosphate alpha-D-glucosyltransferase;
GN   OrderedLocusNames=XCC4077;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   PATHWAY.
RX   PubMed=24055472; DOI=10.1016/j.febslet.2013.09.014;
RA   Nihira T., Saito Y., Nishimoto M., Kitaoka M., Igarashi K., Ohtsubo K.,
RA   Nakai H.;
RT   "Discovery of cellobionic acid phosphorylase in cellulolytic bacteria and
RT   fungi.";
RL   FEBS Lett. 587:3556-3561(2013).
CC   -!- FUNCTION: Catalyzes the reversible phosphorolysis of cellobionic acid
CC       (4-O-beta-D-glucopyranosyl-D-gluconate), a probable step in cellulose
CC       degradation. May be part of a metabolic pathway where cellobionic acid
CC       is converted into alpha-D-glucose 1-phosphate and D-gluconic acid to
CC       enter glycolysis and the pentose phosphate pathway, respectively.
CC       Produces 4-O-beta-D-glucopyranosyl-D-glucuronate from alpha-D-glucose
CC       1-phosphate and D-glucuronate with low activity in the synthetic
CC       direction. {ECO:0000269|PubMed:24055472}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-O-beta-D-glucopyranosyl-D-gluconate + phosphate = alpha-D-
CC         glucose 1-phosphate + D-gluconate; Xref=Rhea:RHEA:11564,
CC         ChEBI:CHEBI:18391, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601,
CC         ChEBI:CHEBI:76825; EC=2.4.1.321;
CC         Evidence={ECO:0000269|PubMed:24055472};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.0 mM for D-gluconate {ECO:0000269|PubMed:24055472};
CC         KM=0.19 mM for 4-O-beta-D-glucopyranosyl-D-gluconate
CC         {ECO:0000269|PubMed:24055472};
CC         KM=0.12 mM for phosphate {ECO:0000269|PubMed:24055472};
CC         KM=2.4 mM for D-glucuronate {ECO:0000269|PubMed:24055472};
CC         KM=0.21 mM for alpha-D-glucose 1-phosphate
CC         {ECO:0000269|PubMed:24055472};
CC         Note=kcat is 173 sec(-1) for D-gluconate. kcat is 43 sec(-1) for D-
CC         glucuronate. kcat is 127 sec(-1) for alpha-D-glucose 1-phosphate.;
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000269|PubMed:24055472}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24055472}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 94 family. Cellobionic
CC       acid phosphorylase subfamily. {ECO:0000305}.
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DR   EMBL; AE008922; AAM43298.1; -; Genomic_DNA.
DR   RefSeq; NP_639416.1; NC_003902.1.
DR   AlphaFoldDB; Q8P3J4; -.
DR   SMR; Q8P3J4; -.
DR   STRING; 340.xcc-b100_4278; -.
DR   CAZy; GH94; Glycoside Hydrolase Family 94.
DR   EnsemblBacteria; AAM43298; AAM43298; XCC4077.
DR   KEGG; xcc:XCC4077; -.
DR   PATRIC; fig|190485.4.peg.4369; -.
DR   eggNOG; COG3459; Bacteria.
DR   HOGENOM; CLU_019054_0_0_6; -.
DR   OMA; FPVGYMS; -.
DR   BRENDA; 2.4.1.321; 6708.
DR   SABIO-RK; Q8P3J4; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0030245; P:cellulose catabolic process; TAS:UniProtKB.
DR   CDD; cd11748; GH94N_NdvB_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; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR033432; GH36_catalytic.
DR   InterPro; IPR037814; GH94N_CBAP.
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   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Polysaccharide degradation;
KW   Reference proteome; Transferase.
FT   CHAIN           1..798
FT                   /note="Cellobionic acid phosphorylase"
FT                   /id="PRO_0000430253"
FT   ACT_SITE        481
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   798 AA;  88423 MW;  EF52F9E391F3E804 CRC64;
     MSAASPAPDD LATLMAPSAD GMRYALYSPT AMPTAGGFLW NRRMMVQLTC RGYATAQFMQ
     PEPAKYAHAP LLEARNFMMP EQPYYAHHPG RFFYLKDEDT GALYSVPHEP VRAPAETFEF
     SAGKHDVRWR VRHDGIVVEL CVSLPTDDAV ELWECRVHNQ SGRTRRLSLY PYFPIGYMSW
     MHQSGGYSPE LGGIVCRSVT PYQKVDDYFR QRDFKDCTFL LHEQPPVAWD AQQMAFEGEG
     GLHAPSAVQA EQLGNHDAHY ENPAAALQYR LSLAPDAATV YRFAFGPAKD DAEIAALRAR
     YLSAEGFAAA AQDYAQYLQA GRGCVQIATP DAALDNLVNH WLPRQVFYHG DVNRLTTDPQ
     TRNYLQDHMG MAYLQPATAR AALLHALSQQ EPSGAMPDGI LLVEGAELKY INQVPHTDHC
     VWLPIFLDAY LAETGDVAVL DAVVRTHDGQ ALSVAARLDA AMQWLLDARD ARGLSFIAQG
     DWNDPMNMVG WRGVGVSGWL TVATAYALRL WSGICAANGR SAQATQFGQA VEEVNAAANR
     ELWDGHWYAR GITDDGVRFG IADDEEGRIY LNPQSWALLA GTADAEQRTA LLAAVREQLH
     TPYGPVMLAP AYTHMRDDVG RLTQKWPGAA ENGAVYNHAV AFYLYSLYQI GDADRAWEIL
     RAMLPGPDMA DALQRGHLPV SLPNYYRGAW HQYPRTAGRS SQLFNTGTVA WVYRCVLEGL
     FGLVGDGDAL AVRPQLPSHW PQAQVTRQFR GAQFEVALTR EPGRTQLEVQ VDGVVSPDQR
     VHGIVAGRTY QLQVRLPG