ID GUNA_XANCP Reviewed; 484 AA.
AC P19487;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=Major extracellular endoglucanase;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE Flags: Precursor;
GN Name=engXCA; OrderedLocusNames=XCC3521;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-61.
RX PubMed=2373365; DOI=10.1016/0378-1119(90)90205-6;
RA Gough C.L., Dow J.M., Keen J., Henrissat B., Daniels M.J.;
RT "Nucleotide sequence of the engXCA gene encoding the major endoglucanase of
RT Xanthomonas campestris pv. campestris.";
RL Gene 89:53-59(1990).
RN [2]
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).
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 -!- DOMAIN: The C-terminal region of the protein is not crucial for
CC activity.
CC -!- DOMAIN: The Thr/Pro-rich region (also termed 'hinge') may be a
CC potential site for proteolysis.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; M32700; AAA27612.1; -; Genomic_DNA.
DR EMBL; AE008922; AAM42791.1; -; Genomic_DNA.
DR PIR; JH0158; JH0158.
DR RefSeq; NP_638867.1; NC_003902.1.
DR RefSeq; WP_011038613.1; NC_003902.1.
DR PDB; 4TUF; X-ray; 2.70 A; A/B/C/D=26-371.
DR PDBsum; 4TUF; -.
DR AlphaFoldDB; P19487; -.
DR SMR; P19487; -.
DR STRING; 190485.XCC3521; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR EnsemblBacteria; AAM42791; AAM42791; XCC3521.
DR KEGG; xcc:XCC3521; -.
DR PATRIC; fig|190485.4.peg.3766; -.
DR eggNOG; COG2730; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_020735_1_0_6; -.
DR OrthoDB; 1153097at2; -.
DR BRENDA; 3.2.1.4; 9230.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2373365"
FT CHAIN 26..484
FT /note="Major extracellular endoglucanase"
FT /id="PRO_0000007875"
FT DOMAIN 395..484
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 370..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..399
FT /note="Thr-Pro repeats ('hinge') (Pro-Thr box)"
FT COMPBIAS 378..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CONFLICT 410..484
FT /note="VDNSWNGGYCNRVQVTNTGTASGTWSIAVPVTGTVNNAWNATWSQSGSTLRA
FT SGVDFNRTLAAGATAEFGFCAAS -> ASPVVGSAARKLPAASRLACHWPASSTGWRVW
FT VIAAPSVTWKRPHAARAIERRMRVTRLRRATRLNRGPLPAPAHTTQHAPRL (in
FT Ref. 1; AAA27612)"
FT /evidence="ECO:0000305"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:4TUF"
FT TURN 60..64
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:4TUF"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:4TUF"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 198..212
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4TUF"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4TUF"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:4TUF"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4TUF"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 313..328
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:4TUF"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:4TUF"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:4TUF"
FT HELIX 359..369
FT /evidence="ECO:0007829|PDB:4TUF"
SQ SEQUENCE 484 AA; 52242 MW; 6671AE5BF1B7602A CRC64;
MSIFRTASTL ALATALALAA GPAFSYSINN SRQIVDDSGK VVQLKGVNVF GFETGNHVMH
GLWARNWKDM IVQMQGLGFN AVRLPFCPAT LRSDTMPASI DYSRNADLQG LTSLQILDKV
IAEFNARGMY VLLDHHTPDC AGISELWYTG SYTEAQWLAD LRFVANRYKN VPYVLGLDLK
NEPHGAATWG TGNAATDWNK AAERGSAAVL AVAPKWLIAV EGITDNPVCS TNGGIFWGGN
LQPLACTPLN IPANRLLLAP HVYGPDVFVQ SYFNDSNFPN NMPAIWERHF GQFAGTHALL
LGEFGGKYGE GDARDKTWQD ALVKYLRSKG INQGFYWSWN PNSGDTGGIL RDDWTSVRQD
KMTLLRTLWG TAGNTTPTPT PTPTPTPTPT PTPTPTPTPG TSTFSTKVIV DNSWNGGYCN
RVQVTNTGTA SGTWSIAVPV TGTVNNAWNA TWSQSGSTLR ASGVDFNRTL AAGATAEFGF
CAAS
//
