GUNC_CELFA
ID GUNC_CELFA Reviewed; 1101 AA.
AC P14090; F4H737;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Endoglucanase C;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase C;
DE AltName: Full=Endo-1,4-beta-glucanase C;
DE Flags: Precursor;
GN Name=cenC; OrderedLocusNames=Celf_1537;
OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS NCIMB 8980 / NCTC 7547).
OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Cellulomonas.
OX NCBI_TaxID=590998;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 33-42.
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC
RC 7547;
RX PubMed=1956299; DOI=10.1111/j.1365-2958.1991.tb01896.x;
RA Coutinho J.B., Moser B., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.;
RT "Nucleotide sequence of the endoglucanase C gene (cenC) of Cellulomonas
RT fimi, its high-level expression in Escherichia coli, and characterization
RT of its products.";
RL Mol. Microbiol. 5:1221-1233(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC
RC 7547;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellulomonas fimi ATCC 484.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64, AND PROTEIN SEQUENCE OF 625-641.
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC
RC 7547;
RX PubMed=2604391; DOI=10.1128/aem.55.10.2480-2487.1989;
RA Moser B., Gilkes N.R., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.;
RT "Purification and characterization of endoglucanase C of Cellulomonas fimi,
RT cloning of the gene, and analysis of in vivo transcripts of the gene.";
RL Appl. Environ. Microbiol. 55:2480-2487(1989).
RN [4]
RP DOMAINS CELLULOSE BINDING.
RX PubMed=1375311; DOI=10.1111/j.1365-2958.1992.tb01563.x;
RA Coutinho J.B., Gilkes N.R., Warren R.A.J., Kilburn D.G., Miller R.C. Jr.;
RT "The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose and
RT Sephadex is mediated by the N-terminal repeats.";
RL Mol. Microbiol. 6:1243-1252(1992).
RN [5]
RP DOMAINS IG-LIKE.
RX PubMed=8880921; DOI=10.1002/pro.5560050923;
RA Bateman A., Eddy S.R., Chothia C.;
RT "Members of the immunoglobulin superfamily in bacteria.";
RL Protein Sci. 5:1939-1942(1996).
RN [6]
RP STRUCTURE BY NMR OF 33-184.
RX PubMed=8916925; DOI=10.1021/bi961612s;
RA Johnson P.E., Joshi M.D., Tomme P., Kilburn D.G., McIntosh L.P.;
RT "Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi
RT CenC determined by nuclear magnetic resonance spectroscopy.";
RL Biochemistry 35:14381-14394(1996).
CC -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR EMBL; X57858; CAA40993.1; -; Genomic_DNA.
DR EMBL; CP002666; AEE45671.1; -; Genomic_DNA.
DR EMBL; M29707; AAA23087.1; ALT_TERM; Genomic_DNA.
DR EMBL; M29708; AAA23088.1; ALT_SEQ; Genomic_DNA.
DR PIR; S15271; S15271.
DR RefSeq; WP_013770697.1; NC_015514.1.
DR PDB; 1CX1; NMR; -; A=178-328.
DR PDB; 1GU3; X-ray; 2.30 A; A=33-181.
DR PDB; 1ULO; NMR; -; A=33-184.
DR PDB; 1ULP; NMR; -; A=33-184.
DR PDBsum; 1CX1; -.
DR PDBsum; 1GU3; -.
DR PDBsum; 1ULO; -.
DR PDBsum; 1ULP; -.
DR AlphaFoldDB; P14090; -.
DR SMR; P14090; -.
DR STRING; 590998.Celf_1537; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; CBM4; Carbohydrate-Binding Module Family 4.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PRIDE; P14090; -.
DR EnsemblBacteria; AEE45671; AEE45671; Celf_1537.
DR KEGG; cfi:Celf_1537; -.
DR eggNOG; COG3250; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_006010_0_0_11; -.
DR OMA; YPWHTCE; -.
DR OrthoDB; 1226595at2; -.
DR EvolutionaryTrace; P14090; -.
DR Proteomes; UP000008460; Chromosome.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR004197; Cellulase_Ig-like.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase; Immunoglobulin domain;
KW Polysaccharide degradation; Reference proteome; Repeat; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:1956299"
FT CHAIN 33..1101
FT /note="Endoglucanase C"
FT /id="PRO_0000007946"
FT DOMAIN 64..173
FT /note="CBM-cenC 1"
FT DOMAIN 212..318
FT /note="CBM-cenC 2"
FT DOMAIN 918..1006
FT /note="Ig-like 1"
FT DOMAIN 1008..1097
FT /note="Ig-like 2"
FT REGION 329..880
FT /note="Catalytic"
FT REGION 838..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 506
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 831
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 882
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1ULP"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1GU3"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1GU3"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1GU3"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:1GU3"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1GU3"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1GU3"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:1GU3"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1GU3"
FT STRAND 169..180
FT /evidence="ECO:0007829|PDB:1GU3"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1CX1"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 239..251
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:1CX1"
FT STRAND 315..324
FT /evidence="ECO:0007829|PDB:1CX1"
SQ SEQUENCE 1101 AA; 115216 MW; 1FBAD189CC5F8B5D CRC64;
MVSRRSSQAR GALTAVVATL ALALAGSGTA LAASPIGEGT FDDGPEGWVA YGTDGPLDTS
TGALCVAVPA GSAQYGVGVV LNGVAIEEGT TYTLRYTATA STDVTVRALV GQNGAPYGTV
LDTSPALTSE PRQVTETFTA SATYPATPAA DDPEGQIAFQ LGGFSADAWT FCLDDVALDS
EVELLPHTSF AESLGPWSLY GTSEPVFADG RMCVDLPGGQ GNPWDAGLVY NGVPVGEGES
YVLSFTASAT PDMPVRVLVG EGGGAYRTAF EQGSAPLTGE PATREYAFTS NLTFPPDGDA
PGQVAFHLGK AGAYEFCISQ VSLTTSATPP PGYEPDTGPR VRVNQVGYLP FGPKRATLVT
DAAEPVAWEL RDADGVVVAD GTSEPRGVEP SAAQAVHVLD FSDVTTQGAG YTLVADGETS
RPFDIDGDLY QQLRYDALNY FYLARSGTEI EADVVGEEYA REAGHVGVAP NQGDTDVPCI
GPRDYYDGWT CDYRLDVSGG WYDAGDHGKY VVNGGIAVGQ LLQTYERALH AGTADALADG
TLDVPEHGND VPDVLDEARW ELEWMLSMIV PEGEYAGMVH HKVHDEGWTG LPLLPADDPQ
ARSLHRPSTA ATLNLSAVAA QGARLLEPYD PQLAQTLLEA ARTTWAAAQE HPALYAPGEA
GADGGGAYND SQVADEFYWA AAELYLTTGE DAFATAVTTS PLHTADVFTA DGFGWGSVAA
LGRLDLATVP NELPGLDAVQ SSVVEGAQEY LAAQAGQGFG SLYSPPGGEY VWGSSSQVAN
NLVVVATAYD LTGDERFRAA TLEGLDYLFG RNALNQSYVT GWGEVASHQQ HSRWFAHQLD
PSLPSPPPGS LAGGPNSQAA TWDPTTKAAF PDGCAPSACY VDEIQAWSTN ELTVNWNSAL
SWVASWVADQ GSAEPVPTAP VVTRQPVDAT VALGADATFT AEASGVPAPT VRWQVRAGRG
WKDVAGATGT TLTVRATART DGTRYRAVFT NAAGSVESAV VRLTVERAAP VVTQHPADVR
ARVGTRAVFR AAADGYPTPC VVWQVRWGGG SWRPIPWATS TTLSVPVTVL AAGTEYRAVF
TNAVGTAATE PAELAVQRPR S
