ID K2SYQ9_MACPH Unreviewed; 1702 AA.
AC K2SYQ9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=glucan endo-1,3-beta-D-glucosidase {ECO:0000256|ARBA:ARBA00012780};
DE EC=3.2.1.39 {ECO:0000256|ARBA:ARBA00012780};
GN ORFNames=MPH_00926 {ECO:0000313|EMBL:EKG21755.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG21755.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG21755.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG21755.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000382};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000822};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family.
CC {ECO:0000256|ARBA:ARBA00010730}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG21755.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHHD01000038; EKG21755.1; -; Genomic_DNA.
DR STRING; 1126212.K2SYQ9; -.
DR VEuPathDB; FungiDB:MPH_00926; -.
DR eggNOG; KOG2254; Eukaryota.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_240835_0_0_1; -.
DR InParanoid; K2SYQ9; -.
DR OrthoDB; 817574at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProt.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
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; IPR040720; GH81_C.
DR InterPro; IPR040451; GH81_N.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31983; ENDO-1,3(4)-BETA-GLUCANASE 1; 1.
DR PANTHER; PTHR31983:SF0; ENDO-1,3(4)-BETA-GLUCANASE 2; 1.
DR Pfam; PF17652; Glyco_hydro81C; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF03639; Glyco_hydro_81; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 1..277
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 480..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1702 AA; 180047 MW; 56CEF53A92E6BB93 CRC64;
MTVITDSYGQ PQINFANQGN KCTVFSGTAL FYCSELEEDI TTCQQTHGKT ITLSIGGATY
SEGGFSSTSE AQAAAELVWA TFGPNQNKSI TSDGTKIYRP FGDASVDGFD FDFESTVSNM
APFAQALRSL MDATEATDGK HRLLTAAPQC PFPDAADDQF LSGALAVKMD AVFVQFYNNY
CGVQSFVSGS STQNNFNFEA WDKWAKSSKN PAVKVFLGVP ASSTAAGSGY LSTSALKPII
DYCMTFPSFG GVMMWDVSQA YANSGFLAAI KHQKPGYCLD YSLQLKLVIG SDGIDIERHQ
HAEPRYASHV ERHFHQFVRA NNGKSMYTSS EQDFDCFLYE YTCRVEQFKQ DNLYKPDGIQ
HAYKQLCRYF FYRNRGSLFQ WNFHHLEHLP DQFRPTFNVS TTGLSLPSFN LSTGLPSRIS
LNFSTGFSSP TSFNNVTRDP VSTAVSSSVI LRSTAQSSGA ELPVSSSGIY LNTTATMTPR
TSVSAVSTDG HSEIMEPSGS AAPTASFTLI AAYNSSSTAP NRFTFFGNTT LPAASATPEP
GRPYSTRSTL SDNSSALSSG ISKFPNTTYT DTAPHTVATT ESTRNAVPPS SSAIVTFGSS
GVLGTSSYRG TSTEGGRSSE VLLTQNSTGT WTTSNPPMLF SSHAITATAY STFAGVSGTN
GTVGASQALA PTLMVSMQTS ASAKAAGAST GSSDLPKPSL ESEPHKMTVS TNPGSSGVSF
STVSSVGLGV TSGSTWSGVS SNTTTSATHS IRTSGVPEIP ISTTGAIKGA NSSTPSGGIF
QTGVVSNTLG ISTSLVTATS SSVISNSARI SVITSIVTVT EHAPGVCSNT HSLSAVATMS
SERYVATESP ATTAANTHSS TLEIPENAQT SVYTSSKAIP STSSTWPGTQ VISIESQVTP
TTQTPVSTPS TTAPPTTSAP VTLEPYPQVT VQPPWPIPPV ANTTSAVVSS PIPVSTCASN
YTYSAVRLCN GKDCNNSIAS TNIFAATSDD PPPSNIRRRS DHPVSRSAIS ADTTGPLHTN
KFYANFFLSE QASGTWTHPY SLSWASGSSG AAQSRGLAIS HIDRSQFVFG DTTAHNSSRY
FFAPLGIQSL ILSAGELSSS TTLRVSAPTA MSANITLAAD GASLPLITFP LVQGMAYVTG
VYRNATPLVE SSVYFRSVEG PIKLHPSSNN NSATIKYRAL LEDGRTWLIY ASPAPGSGYP
VLALANTTRL SGPSGWNGAI SVAKLPVNGT TDDEAIYDSA AGVYPVGAEV FGSASGSTGT
YGFNFTRGGY ATSSASPLLM FALPHHAASF DASTAGGRTS VTLATTTKGY AVAYRGDAWT
MREALAADLG FAPYSAAKGQ SVTALSAGAA CAVIDAAAAE LAQDVGAQTA LDSMYFSGKA
LAKFAAVVYA ANDLGGSAEL AAEGLKKLKA AFAVFVDNRQ PNPLVYDEVW GGVVSNAGYA
DANADFGNSY YNDHHFHYGY FIYTAAVIAY LDPTWLAAGT NKAWTNMLAR DFASPVQNSH
YPSSRSFDWF HGHSWAKGLF SSGDGKDQES SSEDAFASYA LKMWGKVTGD TAMEARGALM
LAIQARSFQS YFLMTRDNTI QPREIINNKV SGVLFENKVD WATYFGDKWY YKEGIHMIPV
HVPSALIRTA EFVAEEYDTY MSGRRIDEAE GGWRGILQAN LALVDAKEAY DYFASANFST
EYLDGGASRT WYLAYTAALA GL
//
