ID   GUNA_FIBSU              Reviewed;         453 AA.
AC   P23665; P23664;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   28-JUN-2023, entry version 89.
DE   RecName: Full=Endoglucanase A;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=endA;
OS   Fibrobacter succinogenes (Bacteroides succinogenes).
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AR1;
RX   PubMed=1708767; DOI=10.1128/jb.173.10.3265-3268.1991;
RA   Cavicchioli R., East P.D., Watson K.;
RT   "endAFS, a novel family E endoglucanase gene from Fibrobacter succinogenes
RT   AR1.";
RL   J. Bacteriol. 173:3265-3268(1991).
RN   [2]
RP   RIBOSOMAL FRAMESHIFT.
RC   STRAIN=AR1;
RX   PubMed=2027774; DOI=10.1093/nar/19.7.1661;
RA   Cavicchioli R., Watson K.;
RT   "The involvement of transcriptional read-through from internal promoters in
RT   the expression of a novel endoglucanase gene FSendA, from Fibrobacter
RT   succinogenes AR1.";
RL   Nucleic Acids Res. 19:1661-1669(1991).
RN   [3]
RP   SUBSTRATES, SUBUNIT, SUBCELLULAR LOCATION, AND CHARACTERIZATION.
RC   STRAIN=AR1;
RX   PubMed=2014986; DOI=10.1128/aem.57.2.359-365.1991;
RA   Cavicchioli R., Watson K.;
RT   "Molecular cloning, expression, and characterization of endoglucanase genes
RT   from Fibrobacter succinogenes AR1.";
RL   Appl. Environ. Microbiol. 57:359-365(1991).
CC   -!- FUNCTION: High levels of endoglucanase activity detected on acid-
CC       swollen cellulose, ball-milled cellulose, and carboxymethyl cellulose;
CC       moderate levels detected on filter paper, phosphoric acid-swollen
CC       cellulose, lichenan, and xylan.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0.;
CC       Temperature dependence:
CC         Optimum temperature is 37-39 degrees Celsius.;
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:2014986}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2014986}. Note=80%
CC       periplasmic, 16% extracellular upon overexpression in E.coli.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC   -!- CAUTION: Expression of endA requires a ribosomal frameshift to allow
CC       contiguous translation of a 453 amino acid protein; this is suggested
CC       to take place at position 127 but could in fact occur anywhere between
CC       positions 82 and 127. {ECO:0000305}.
CC   -!- CAUTION: On the basis of sequence similarities the C-terminal part of
CC       this sequence seems to be incorrect. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA24895.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M58520; AAA24894.1; -; Genomic_DNA.
DR   EMBL; M58520; AAA24895.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A39416; A39416.
DR   AlphaFoldDB; P23665; -.
DR   SMR; P23665; -.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS60032; GH9_1; 1.
DR   PROSITE; PS00592; GH9_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Periplasm; Polysaccharide degradation; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..453
FT                   /note="Endoglucanase A"
FT                   /id="PRO_0000007954"
FT   REGION          115..126
FT                   /note="Linker ('hinge') (Pro-Thr box)"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        417
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
SQ   SEQUENCE   453 AA;  50042 MW;  7E861B76070D1186 CRC64;
     MNCRKYLLSG LAVFGLAATS AVAALSTDDY VEAAWMTTRF FGAQRSGQGP NWILDGTSNP
     TSFTKDSYNG KDVSGGWFDC GDHVMYGQSQ GYASYVLALA YAEFTEVSTT FILVTTPTTR
     KPTTTPMKSG KPNKVRDLLE ELRYEADFWV KAAIDGNNFV TVKGDGNADH QKWVTAGAMS
     KLGSGEGGEP RCITGNANDG FTSGLAAAML AVMARVDPDT ANQAKYLKAA KTAYSYAKSH
     KGVTNSQGFY ESSWWDGRWE DGPFLAELEL YRTTGENSYK TAAIDRYDNL KFSLGEGTHF
     MYSNVVPLSA VMAEAVFEET PHGMRKEAIG VLDLIYEEKA KDKIFQNPNG MGSGKFPVRV
     PSGGAFLYAL SDKFNNTNEH MEMIEKNVSY LLGDNGSKKS YVVGFSKNGA NAPSRPHHRG
     YYANEKRWRR SRRCSESSRK EQALGRYDCW RLY
//