GUNA_CALSA
ID GUNA_CALSA Reviewed; 1742 AA.
AC P22534;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Endoglucanase A;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase A;
DE AltName: Full=Endo-1,4-beta-glucanase A;
DE Flags: Precursor;
GN Name=celA;
OS Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX NCBI_TaxID=44001;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7612247; DOI=10.1007/bf00172827;
RA Te'O V.S. Jr., Saul D.J., Bergquist P.L.;
RT "celA, another gene coding for a multidomain cellulase from the extreme
RT thermophile Caldocellum saccharolyticum.";
RL Appl. Microbiol. Biotechnol. 43:291-296(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1516-1742.
RX PubMed=2039230; DOI=10.1128/aem.57.3.694-700.1991;
RA Luethi E., Jasmat N.B., Grayling R.A., Love D.R., Bergquist P.L.;
RT "Cloning, sequence analysis, and expression in Escherichia coli of a gene
RT coding for a beta-mannanase from the extremely thermophilic bacterium
RT 'Caldocellum saccharolyticum'.";
RL Appl. Environ. Microbiol. 57:694-700(1991).
CC -!- FUNCTION: The N-terminal domain of CelA codes for an endoglucanase
CC activity on carboxymethylcellulose. The C-terminal domain probably acts
CC synergistically to hydrolyze crystalline cellulose.
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 -!- PTM: The linker region (also termed 'hinge') may be a potential site
CC for proteolysis.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 48 (cellulase L) family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
CC hydrolase 9 (cellulase E) family. {ECO:0000255|PROSITE-
CC ProRule:PRU10140, ECO:0000305}.
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DR EMBL; L32742; AAA91086.1; -; Genomic_DNA.
DR EMBL; M36063; AAA72860.1; -; Genomic_DNA.
DR EMBL; L01257; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR PIR; T17120; T17120.
DR AlphaFoldDB; P22534; -.
DR SMR; P22534; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH48; Glycoside Hydrolase Family 48.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR BRENDA; 3.2.1.4; 1055.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 2.
DR Gene3D; 2.170.160.10; -; 1.
DR Gene3D; 2.60.40.710; -; 3.
DR Gene3D; 4.10.870.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2.
DR InterPro; IPR027390; Endoglucanase_F_dom3.
DR InterPro; IPR000556; Glyco_hydro_48F.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR Pfam; PF00942; CBM_3; 3.
DR Pfam; PF02011; Glyco_hydro_48; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR PRINTS; PR00844; GLHYDRLASE48.
DR SMART; SM01067; CBM_3; 3.
DR SUPFAM; SSF48208; SSF48208; 2.
DR SUPFAM; SSF49384; SSF49384; 3.
DR PROSITE; PS51172; CBM3; 3.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Repeat; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1742
FT /note="Endoglucanase A"
FT /id="PRO_0000007944"
FT DOMAIN 477..637
FT /note="CBM3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT DOMAIN 703..856
FT /note="CBM3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT DOMAIN 906..1059
FT /note="CBM3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT REGION 24..476
FT /note="Catalytic 1"
FT REGION 634..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..702
FT /note="Linker ('hinge') (Pro-Thr box)"
FT REGION 855..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..905
FT /note="Linker ('hinge') (Pro-Thr box)"
FT REGION 1059..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1112
FT /note="Linker ('hinge') (Pro-Thr box)"
FT REGION 1113..1742
FT /note="Catalytic 2"
FT COMPBIAS 648..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..899
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 434
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CONFLICT 1545
FT /note="T -> A (in Ref. 2; AAA72860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1742 AA; 193697 MW; 3F0699A2123EED07 CRC64;
MVVTFLFILG VVYGVKPWQE ARAGSFNYGE ALQKAIMFYE FQMSGKLPNW VRNNWRGDSA
LKDGQDNGLD LTGGWFDAGD HVKFNLPMSY TGTMLSWAAY EYKDAFVKSG QLEHILNQIE
WVNDYFVKCH PSKYVYYYQV GDGGKDHAWW GPAEVMQMER PSFKVTQSSP GSAVVAETAA
SLAAASIVLK DRNPTKAATY LQHAKDLYEF AEVTKSDSGY TAANGYYNSW SGFYDELSWA
AVWLYLATND STYLTKAESY VQNWPKISGS NIIDYKWAHC WDDVHNGAAL LLAKITDKDT
YKQIIESHLD YWTTGYNGER IKYTPKGLAW LDQWGSLRYA TTTAFLAFVY SDWSGCPTGK
KETYRKFGES QIDYALGSTG RSFVVGFGTN PPKRPHHRTA HSSWADSQSI PSYHRHTLYG
ALVGGPGSDD SYTDDISNYV NNEVACDYNA GFVGALAKMY LLYGGNPIPD FKAIETPTND
EFFVEAGINA SGTNFIEIKA IVNNQSGWPA RATNKLKFRY FVDLSELIKA GYSPNQLTLS
TNYNQGAKVS GPYVWDSSRN IYYILVDFTG TLIYPGGQDK YKKEVQFRIA APQNVQWDNS
NDYSFQDIKG VSSGSVVKTK YIPLYDEDIK VWGEEPGTSG VSPTPTASVT PTPTPTPTAT
PTPTPTPTVT PTPTVTATPT PTPTPTSTPT VTPTPTPVST PATSGQIKVL YANKETNSTT
NTIRPWLKVV NSGSSSIDLS RVTIRYWYTV DGERAQSAIS DWAQIGASNV TFKFVKLSSS
VSGADYYLEI GFKSGAGQLQ PGKDTGEIQI RFNKDDWSNY NQGNDWSWIQ SMTSYGENEK
VTAYIDGVLV WGQEPSGTTP APTSTPTVTV TPTPTPTPTV TPTPTVTATP TPTPTPTSTP
VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI DLSRVTIRYW YTVDGERAQS
AISDWAQIGA SNVTFKFVKL SSSVSGADYY LEIGFKSGAG QLQPGKDTGE IQIRFNKDDW
SNYNQGNDWS WIQSMTSYGE NEKVTAYIDG VLVWGQEPSG ATPAPTVTPT PTVTPTPTPA
PTPTATPTPT PTPTVTPTPT VAPTPTPSST PSGLGKYGQR FMWLWNKIHD PASGYFNQDG
IPYHSVETLI CEAPDYGHLT TSEAFSYYVW LEAVYGKLTG DWSKFKTAWD TLEKYMIPSA
EDQPMRSYDP NKPATYAGEW ETPDKYPSPL EFNVPVGKDP LHNELVSTYG STLMYGMHWL
MDVDNWYGYG KRGDGVSRAS FINTFQRGPE ESVWETVPHP SWEEFKWGGP NGFLDLFIKD
QNYSKQWRYT NAPDADARAI QATYWAKVWA KEQGKFNEIS SYVGKAAKMG DYLRYAMFDK
YFKPLGCQDK NAAGGTGYDS AHYLLSWYYA WGGALDGAWS WKIGCSHAHF GYQNPMAAWA
LANDSDMKPK SPNGASDWAK SLKRQIEFYR WLQSAEGAIA GGATNSWNGR YEKYPAGTAT
FYGMAYEPNP VYRDPGSNTW FGFQAWSMQR VAEYYYVTGD KDAGTLLEKW VSWIKSVVKL
NSDGTFAIPS TLDWSGQPDT WNGTYTGNPN LHVKVVDYGT DLGITASLAN ALLYYSAGTK
KYGVFDEEAK NLAKELLDRM WKLYRDEKGL SAPEKRADYK RFFEQEVYIP AGWTGKMPNG
DVIKSGVKFI DIRSKYKQDP DWPKLEAAYK SGQVPEFRYH RFWAQCDIAI VNATYEILFG
NQ
