EGLX_EMENI
ID EGLX_EMENI Reviewed; 626 AA.
AC Q5BAP5; C8VNP1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Endo-1,3(4)-beta-glucanase xgeA;
DE EC=3.2.1.6;
DE AltName: Full=Mixed-linked glucanase xgeA;
DE Flags: Precursor;
GN Name=xgeA; ORFNames=AN2385;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
CC -!- FUNCTION: Mixed-linked glucanase involved in the degradation of complex
CC natural cellulosic substrates. Active on laminarin. lichenan, soluble
CC carboxymethyl cellulose but not on pustulan.
CC {ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans
CC when the glucose residue whose reducing group is involved in the
CC linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; AACD01000039; EAA64496.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF86736.1; -; Genomic_DNA.
DR RefSeq; XP_659989.1; XM_654897.1.
DR AlphaFoldDB; Q5BAP5; -.
DR SMR; Q5BAP5; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR CLAE; MLG16A_EMENI; -.
DR EnsemblFungi; CBF86736; CBF86736; ANIA_02385.
DR EnsemblFungi; EAA64496; EAA64496; AN2385.2.
DR GeneID; 2874796; -.
DR KEGG; ani:AN2385.2; -.
DR VEuPathDB; FungiDB:AN2385; -.
DR eggNOG; ENOG502QUM3; Eukaryota.
DR HOGENOM; CLU_016972_4_0_1; -.
DR InParanoid; Q5BAP5; -.
DR OMA; ILNINFC; -.
DR OrthoDB; 754530at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0042972; F:licheninase activity; IDA:UniProtKB.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell membrane; Cellulose degradation;
KW Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..603
FT /note="Endo-1,3(4)-beta-glucanase xgeA"
FT /id="PRO_0000395093"
FT PROPEP 604..626
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395094"
FT DOMAIN 33..286
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 477..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 603
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 626 AA; 65098 MW; B18C705CD41F4045 CRC64;
MSSSLMRRVG SLAASAIIFP GIAHAASNYK LKESWEGEKI LNHFHFFDNA DPTNGFVTYV
NQSYAESAGL VKTTDSGSLY LGVDYENVLT VDGPGRESVR IESNEYYDQG LYVVDIQHMP
GSICGTWPAF WTVGPDWPTD GEIDIIEGVN KHDANKIVLH TSDTCDVGGG YKMTGDMTSS
ECGEASGTIG CVVQGKQGSS GDPFNEQGGG VYAMEWQEKY LKIWYFPRSS IPESLTAGTP
DVSSFGTPMA HLQGSCNFKE RFTHQKLILD TTFCGDWAGG VFGDSGCPVS DPSDPMLSCK
NYVAENPAVY KNAYWELNSI KIYQLGGTAE VEGTQSAAAE STAAEATAAE TTAAATQTAN
GGSIEEITTS THSVTRTKTV SATHSTETAA VTETAAATTA AASVASEVDA TNTQPVSKTK
STSYVTSTTT LCPVESSQAA ATESVSRTKT TSYVTITTTL CPVESLQTAN AVPSAKASTD
AAAATTPAAE PHPSNAETPA DSKSSADAVT AQATKTTIAV NTPNPATDSA SSVPPDSIVY
TAPEVTSSSS VPLFTIVSSS SQFVTVPTAA PSSFEPTDAV RDGADSYSTA ASPTTPSNPV
FTGVGSKVSI SASVAIAAFV MLLLVN
