GUNF_RUMCH
ID GUNF_RUMCH Reviewed; 722 AA.
AC P37698; B8I7V1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Endoglucanase F;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase F;
DE AltName: Full=EGCCF;
DE AltName: Full=Endo-1,4-beta-glucanase F;
DE Flags: Precursor;
GN Name=celCCF; OrderedLocusNames=Ccel_0729;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8936327; DOI=10.1099/00221287-142-4-1013;
RA Reverbel-Leroy C., Belaich A., Bernadac A., Gaudin C., Belaich J.-P.,
RA Tardif C.;
RT "Molecular study and overexpression of the Clostridium cellulolyticum celF
RT cellulase gene in Escherichia coli.";
RL Microbiology 142:1013-1023(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 387-722.
RX PubMed=1398087; DOI=10.1016/0378-1119(92)90062-t;
RA Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T.,
RA Belaich J.-P.;
RT "Sequence analysis of a gene cluster encoding cellulases from Clostridium
RT cellulolyticum.";
RL Gene 119:17-28(1992).
CC -!- FUNCTION: Probable endoglucanase involved in the degradation of
CC cellulose or related beta-glucans.
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 48 (cellulase L) family.
CC {ECO:0000305}.
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DR EMBL; U30321; AAB41452.1; -; Genomic_DNA.
DR EMBL; CP001348; ACL75108.1; -; Genomic_DNA.
DR EMBL; M87018; AAA73866.1; -; Genomic_DNA.
DR PIR; PC1139; PC1139.
DR RefSeq; WP_015924275.1; NC_011898.1.
DR PDB; 1F9D; X-ray; 2.30 A; A=30-658.
DR PDB; 1F9O; X-ray; 2.50 A; A=30-658.
DR PDB; 1FAE; X-ray; 2.00 A; A=30-658.
DR PDB; 1FBO; X-ray; 2.30 A; A=30-658.
DR PDB; 1FBW; X-ray; 2.00 A; A=30-658.
DR PDB; 1FCE; X-ray; 2.00 A; A=30-658.
DR PDB; 1G9G; X-ray; 1.90 A; A=30-658.
DR PDB; 1G9J; X-ray; 1.90 A; A=30-658.
DR PDB; 2QNO; X-ray; 2.00 A; A=30-658.
DR PDBsum; 1F9D; -.
DR PDBsum; 1F9O; -.
DR PDBsum; 1FAE; -.
DR PDBsum; 1FBO; -.
DR PDBsum; 1FBW; -.
DR PDBsum; 1FCE; -.
DR PDBsum; 1G9G; -.
DR PDBsum; 1G9J; -.
DR PDBsum; 2QNO; -.
DR AlphaFoldDB; P37698; -.
DR SMR; P37698; -.
DR STRING; 394503.Ccel_0729; -.
DR DrugBank; DB03857; 1,4-dithio-beta-D-glucopyranose.
DR DrugBank; DB03584; 4-Thio-beta-D-glucopyranose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB02252; Iodobenzene.
DR DrugBank; DB01642; methyl beta-D-glucopyranoside.
DR CAZy; GH48; Glycoside Hydrolase Family 48.
DR EnsemblBacteria; ACL75108; ACL75108; Ccel_0729.
DR KEGG; cce:Ccel_0729; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_009014_1_0_9; -.
DR OMA; QWFGFQA; -.
DR OrthoDB; 191946at2; -.
DR BRENDA; 3.2.1.4; 1468.
DR EvolutionaryTrace; P37698; -.
DR Proteomes; UP000001349; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.170.160.10; -; 1.
DR Gene3D; 4.10.870.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2.
DR InterPro; IPR027390; Endoglucanase_F_dom3.
DR InterPro; IPR000556; Glyco_hydro_48F.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF02011; Glyco_hydro_48; 1.
DR PRINTS; PR00844; GLHYDRLASE48.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..722
FT /note="Endoglucanase F"
FT /id="PRO_0000008026"
FT DOMAIN 661..722
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT REGION 142..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:1G9G"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2QNO"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 258..276
FT /evidence="ECO:0007829|PDB:1G9G"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 374..391
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:1G9G"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 424..429
FT /evidence="ECO:0007829|PDB:1G9G"
FT TURN 433..438
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 442..458
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 461..475
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 486..496
FT /evidence="ECO:0007829|PDB:1G9G"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 514..521
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 524..541
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 544..560
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:1G9G"
FT TURN 574..577
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 611..615
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 619..627
FT /evidence="ECO:0007829|PDB:1G9G"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:1G9G"
FT HELIX 639..655
FT /evidence="ECO:0007829|PDB:1G9G"
SQ SEQUENCE 722 AA; 80544 MW; 5E48F85319D70AE5 CRC64;
MSKNFKRVGA VAVAAAMSLS IMATTSINAA SSPANKVYQD RFESMYSKIK DPANGYFSEQ
GIPYHSIETL MVEAPDYGHV TTSEAMSYYM WLEAMHGRFS GDFTGFDKSW SVTEQYLIPT
EKDQPNTSMS RYDANKPATY APEFQDPSKY PSPLDTSQPV GRDPINSQLT SAYGTSMLYG
MHWILDVDNW YGFGARADGT SKPSYINTFQ RGEQESTWET IPQPCWDEHK FGGQYGFLDL
FTKDTGTPAK QFKYTNAPDA DARAVQATYW ADQWAKEQGK SVSTSVGKAT KMGDYLRYSF
FDKYFRKIGQ PSQAGTGYDA AHYLLSWYYA WGGGIDSTWS WIIGSSHNHF GYQNPFAAWV
LSTDANFKPK SSNGASDWAK SLDRQLEFYQ WLQSAEGAIA GGATNSWNGR YEAVPSGTST
FYGMGYVENP VYADPGSNTW FGMQVWSMQR VAELYYKTGD ARAKKLLDKW AKWINGEIKF
NADGTFQIPS TIDWEGQPDT WNPTQGYTGN ANLHVKVVNY GTDLGCASSL ANTLTYYAAK
SGDETSRQNA QKLLDAMWNN YSDSKGISTV EQRGDYHRFL DQEVFVPAGW TGKMPNGDVI
KSGVKFIDIR SKYKQDPEWQ TMVAALQAGQ VPTQRLHRFW AQSEFAVANG VYAILFPDQG
PEKLLGDVNG DETVDAIDLA ILKKYLLNSS TTINTANADM NSDNAIDAID YALLKKALLS
IQ
