ID   ENG1_SCHPO              Reviewed;        1016 AA.
AC   Q9UT45; Q9UTZ1;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Primary septum glucan endo-1,3-beta-D-glucosidase {ECO:0000303|PubMed:19542306};
DE   AltName: Full=Glucan endo-1,3-beta-D-glucosidase 1;
DE            Short=Endo-1,3-beta-glucanase 1;
DE            EC=3.2.1.39 {ECO:0000305|PubMed:12665550};
DE   AltName: Full=Laminarinase-1;
DE   Flags: Precursor;
GN   Name=eng1 {ECO:0000303|PubMed:12665550,
GN   ECO:0000312|PomBase:SPAC821.09};
GN   ORFNames=SPAC821.09 {ECO:0000312|PomBase:SPAC821.09};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-168, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=12665550; DOI=10.1242/jcs.00377;
RA   Martin-Cuadrado A.B., Duenas E., Sipiczki M., de Aldana C.R.V., del Rey F.;
RT   "The endo-beta-1,3-glucanase eng1p is required for dissolution of the
RT   primary septum during cell separation in Schizosaccharomyces pombe.";
RL   J. Cell Sci. 116:1689-1698(2003).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18466295; DOI=10.1111/j.1365-2958.2008.06275.x;
RA   Martin-Cuadrado A.B., Encinar del Dedo J., de Medina-Redondo M.,
RA   Fontaine T., del Rey F., Latge J.P., Vazquez de Aldana C.R.;
RT   "The Schizosaccharomyces pombe endo-1,3-beta-glucanase Eng1 contains a
RT   novel carbohydrate binding module required for septum localization.";
RL   Mol. Microbiol. 69:188-200(2008).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19542306; DOI=10.1128/ec.00148-09;
RA   Encinar del Dedo J., Duenas E., Arnaiz Y., del Rey F.,
RA   Vazquez de Aldana C.R.;
RT   "{beta}-glucanase Eng2 is required for ascus wall endolysis after
RT   sporulation in the fission yeast Schizosaccharomyces pombe.";
RL   Eukaryot. Cell 8:1278-1286(2009).
CC   -!- FUNCTION: Cleaves internal linkages in 1,3-beta-glucan (Probable). Has
CC       a role in cell separation where it is required for the degradation of
CC       the primary septum after completion of cytokinesis (PubMed:12665550,
CC       PubMed:18466295). {ECO:0000269|PubMed:12665550,
CC       ECO:0000269|PubMed:18466295, ECO:0000305|PubMed:12665550}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000305|PubMed:12665550};
CC   -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000269|PubMed:10759889,
CC       ECO:0000269|PubMed:12665550, ECO:0000269|PubMed:18466295}.
CC       Note=Localized in a ring-like structure around the septum.
CC       {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12665550,
CC       ECO:0000269|PubMed:18466295}.
CC   -!- DISRUPTION PHENOTYPE: Decreases basal endo-1,3-beta-glucanase activity
CC       (PubMed:19542306). Cells do not separate normally after cytokinesis
CC       resulting in chained cells (PubMed:18466295).
CC       {ECO:0000269|PubMed:18466295, ECO:0000269|PubMed:19542306}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01352, ECO:0000305}.
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DR   EMBL; CU329670; CAB57443.1; -; Genomic_DNA.
DR   EMBL; AB027918; BAA87222.1; ALT_SEQ; Genomic_DNA.
DR   PIR; T41720; T41720.
DR   RefSeq; NP_593162.1; NM_001018560.2.
DR   AlphaFoldDB; Q9UT45; -.
DR   SMR; Q9UT45; -.
DR   BioGRID; 279801; 17.
DR   STRING; 284812.Q9UT45; -.
DR   CAZy; CBM52; Carbohydrate-Binding Module Family 52.
DR   CAZy; GH81; Glycoside Hydrolase Family 81.
DR   CLAE; LAM81A_SCHPO; -.
DR   GlyCosmos; Q9UT45; 1 site, No reported glycans.
DR   iPTMnet; Q9UT45; -.
DR   MaxQB; Q9UT45; -.
DR   PaxDb; 4896-SPAC821-09-1; -.
DR   EnsemblFungi; SPAC821.09.1; SPAC821.09.1:pep; SPAC821.09.
DR   GeneID; 2543379; -.
DR   KEGG; spo:SPAC821.09; -.
DR   PomBase; SPAC821.09; eng1.
DR   VEuPathDB; FungiDB:SPAC821.09; -.
DR   eggNOG; KOG2254; Eukaryota.
DR   HOGENOM; CLU_005482_2_1_1; -.
DR   InParanoid; Q9UT45; -.
DR   OMA; FMNKITH; -.
DR   PhylomeDB; Q9UT45; -.
DR   PRO; PR:Q9UT45; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0009986; C:cell surface; IDA:PomBase.
DR   GO; GO:0000935; C:division septum; IDA:PomBase.
DR   GO; GO:1990819; C:mating projection actin fusion focus; IDA:PomBase.
DR   GO; GO:0000936; C:primary cell septum; IDA:PomBase.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:PomBase.
DR   GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR   GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IDA:PomBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0044347; P:cell wall polysaccharide catabolic process; IC:PomBase.
DR   GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IMP:PomBase.
DR   GO; GO:0030994; P:primary cell septum disassembly; IMP:UniProtKB.
DR   Gene3D; 1.10.287.1170; glycoside hydrolase family 81 endo-[beta] glucanase; 1.
DR   Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1.
DR   InterPro; IPR005200; Endo-beta-glucanase.
DR   InterPro; IPR018909; Eng1_septum.
DR   InterPro; IPR040720; GH81_C.
DR   InterPro; IPR040451; GH81_N.
DR   PANTHER; PTHR31983; ENDO-1,3(4)-BETA-GLUCANASE 1; 1.
DR   PANTHER; PTHR31983:SF21; PRIMARY SEPTUM ENDO-1,3(4)-BETA-GLUCANASE; 1.
DR   Pfam; PF10645; Carb_bind; 3.
DR   Pfam; PF17652; Glyco_hydro81C; 1.
DR   Pfam; PF03639; Glyco_hydro_81; 1.
DR   PROSITE; PS52008; GH81; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell cycle; Cell division;
KW   Cell wall biogenesis/degradation; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1016
FT                   /note="Primary septum glucan endo-1,3-beta-D-glucosidase"
FT                   /id="PRO_0000012132"
FT   DOMAIN          45..741
FT                   /note="GH81"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"
FT   REGION          45..272
FT                   /note="beta-sandwich subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"
FT   REGION          273..364
FT                   /note="alpha/beta subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"
FT   REGION          379..741
FT                   /note="(alpha/beta)6 barrel subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"
FT   REGION          748..1016
FT                   /note="Required for catalytic activity against insoluble
FT                   beta-glucan and to restrict localization of the enzyme to
FT                   the cell septum"
FT                   /evidence="ECO:0000269|PubMed:18466295"
FT   REGION          844..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        492
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"
FT   ACT_SITE        569
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"
FT   ACT_SITE        573
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01352"
FT   BINDING         496
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /evidence="ECO:0000250|UniProtKB:A0A023I7E1"
FT   BINDING         567
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /evidence="ECO:0000250|UniProtKB:A0A023I7E1"
FT   BINDING         569
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /evidence="ECO:0000250|UniProtKB:A0A023I7E1"
FT   BINDING         573
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /evidence="ECO:0000250|UniProtKB:A0A023I7E1"
FT   BINDING         650
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /evidence="ECO:0000250|UniProtKB:A0A023I7E1"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1016 AA;  109743 MW;  9240CA34D35786FC CRC64;
     MSSYLRSFIF GLLTISLAQC SPILKDTKDT KFSTGSNISL KKRDTNVFDS VVDTINPASY
     FGTVSHPVTP AGVSTDSLSS PIETNKFFDN NLLGSRTNFM YADPFRYWWQ SSDTMGGICI
     AHTDDNQRVM DTDDTIPSYY YEPIGICSLG FGASGITSNT DPIVDEIDQM SARFTFSWDS
     SSMQLTLTEG MAVTTAVYTN AIPQIFSSTL YINDFVEVPG TSAVQKYRVT MSDNHVWLIY
     IYGDSLTLTE STSQMLVGSN TFNGYIQIAK IPLGDGTAEA LYDTYAGVYI TGISISGYVE
     DAVGYYSFDF TTAGDTSVEP LFFLLPHQVD TAVSGTKVTS IVLASLVSGD MNAAAGNSIT
     FAEAIPQDIG FLPWSPTGGQ IGYSEEALEI IAEVAGTELG EDFSANSNLN SMYYSGKVLA
     KYAMLCVTIN DILGDETSSE QCIQKLEAAF ARFVDNQQIY PLTYDNTWKG VVSVAGLSGD
     SLADFGNSYY NDHHFHYGYF VFTAAVIGHI DPDWINTGNN KEWVNFLVRD VANPSSNDPY
     FPKHRMIDIY HGHGWASGLF ESNDGKDEES TSEDYNFFFG MKLWGQVIGD SDMEDRANII
     LGIERNALNK YMLYADGNVQ PTSMQPNYVA GITFMNKITH TTYFGTNIEY IQGIHMLPIT
     PISAFIRGPS FVLAEWNALL ASVIDYVDSG WRSLLYANLA IAEPEESYEY FSSSDFNTDY
     LDDGASRAWY LAYAAGLWAN DAVYYPVSSS STTTTSTSTG SVTTTSTTAT ASCTLPISYT
     STPTTTSISG TCNGATFDAS LYVCDGTVLC PIVNGVSYQN CNGACYNPSQ YGCDNGALGP
     VQSSSTTSSI TPTPTTTSSI TPTPTTTSTT TTAQSTGMQL CGSNYYDASS YYCDNDQLCP
     IIDGVDYLSC NGACYNPSQY VCSDGSLSPN TVTTTKATTT FTPTPTTTTT PTPTTTSATS
     TNVIAQCGSA WYDSQSYICY GNILCPIING SPLLACGNAC YDSSIYGCSN GALVAA
//