ID   CELAP_NEUCR             Reviewed;         791 AA.
AC   Q7S0S2;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 86.
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   ORFNames=NCU09425;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
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=1.0 mM for 4-O-beta-D-glucopyranosyl-D-gluconate
CC         {ECO:0000269|PubMed:24055472};
CC         KM=0.1 mM for phosphate {ECO:0000269|PubMed:24055472};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
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; CM002242; EAA28929.1; -; Genomic_DNA.
DR   RefSeq; XP_958165.1; XM_953072.2.
DR   AlphaFoldDB; Q7S0S2; -.
DR   SMR; Q7S0S2; -.
DR   STRING; 5141.EFNCRP00000009243; -.
DR   CAZy; GH94; Glycoside Hydrolase Family 94.
DR   EnsemblFungi; EAA28929; EAA28929; NCU09425.
DR   GeneID; 3874312; -.
DR   KEGG; ncr:NCU09425; -.
DR   VEuPathDB; FungiDB:NCU09425; -.
DR   HOGENOM; CLU_019054_0_0_1; -.
DR   InParanoid; Q7S0S2; -.
DR   OMA; YVYAQMI; -.
DR   BRENDA; 2.4.1.321; 3627.
DR   SABIO-RK; Q7S0S2; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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..791
FT                   /note="Cellobionic acid phosphorylase"
FT                   /id="PRO_0000430254"
FT   ACT_SITE        475
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   791 AA;  89547 MW;  9475A4848D403732 CRC64;
     MTRKMPTLVR PTHNGERYEI TNPTAMPKAA GFLWNQKMMI QITCRGFATA QFMQPEPAKY
     AYAPNIEAKT FMQPEPNYYA HHPGRFVYIK DEETGRLFSA PYEPVRAPHD RFVFSAGKTD
     VFWVIESMGI RVEMTMGLPT HHVAELWTIK VKNLSSRPRK LSVTPYFPIG YMSWMNQSAE
     WNHNLNGIVA SCVTPYQKAA DYFKNKYLKD KTYFLCDVPP DSWEASQQAF EGEGGLHNPS
     ALQERNLSGS DARYETPTAA VQYKIALGTG EQQEYRFLFG PAHDEAEIGA MRSKYLSKEG
     FEQTAADYAA YMARGRGCLH VETPDKDLDN FINNWLPRQV YYHGDVNRLT TDPQTRNYLQ
     DNMGMNYIKP EVSRRAFLTA IAQQEATGAM PDGILLVEGA ELKYINQVPH TDHCVWLPVT
     LEAYLNETGD YSLLKEKVPS ANGDKLTVFE RFCRAMDWLL KSRDHRGLSY IAQGDWCDPM
     NMVGYKGKGV SGWLTLATAF SLNIWAKVCD HEGETDLAKR FREGADACNA AANEHLWDGE
     WFARGITDDN VVFGIKEDKE GRIWLNPQSW SILSGAASPE QIDKMLPQID SHLNTPYGIQ
     MFGPPYTKMR EDVGRVTQKA IGSAENAAVY NHAGIFFIHS LYELGAQQDR AFTLLRQMLP
     GPTDTDYIQR GQLPIYIPNY YRGAWKECPR TAGRSSQLFN TGTVSWVYRC IIEGLCGLRG
     DGEGLLIRPQ LPSSWNSMKV TREFRGATFN VDIRRGNVKE VTVRNGDKVL PAPHVKDIEP
     GQTYNLTVTI P