ID A0A2U1MU09_ARTAN Unreviewed; 947 AA.
AC A0A2U1MU09;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=CTI12_AA309610 {ECO:0000313|EMBL:PWA64706.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA64706.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA64706.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA64706.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
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 Evidence={ECO:0000256|ARBA:ARBA00000966,
CC ECO:0000256|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000256|ARBA:ARBA00009084}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10059,
CC ECO:0000256|RuleBase:RU361166}.
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:PWA64706.1}.
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; PKPP01004371; PWA64706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1MU09; -.
DR STRING; 35608.A0A2U1MU09; -.
DR Proteomes; UP000245207; Unassembled WGS sequence.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0004333; F:fumarate hydratase activity; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd01362; Fumarase_classII; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR HAMAP; MF_00743; FumaraseC; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR005677; Fum_hydII.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR018951; Fumarase_C_C.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00979; fumC_II; 1.
DR PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR11444:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
DR PROSITE; PS00592; GH9_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|PROSITE-ProRule:PRU10059,
KW ECO:0000256|RuleBase:RU361166};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU10059,
KW ECO:0000256|RuleBase:RU361166};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Reference proteome {ECO:0000313|Proteomes:UP000245207}.
FT DOMAIN 1..403
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT DOMAIN 495..825
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 891..943
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 330
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
SQ SEQUENCE 947 AA; 104547 MW; 43C30F547299968E CRC64;
MAFTVTMLSW SIIEYGEYIA NAGELHHAIE AVKWGTDYFI KAHTSPNVLW AEVGDGDTDH
YCWQRPEDMT TSRQAYRIDE NNPGSDLAGE AAAAMAAASI VFKKTNPHYS HLLLHHAQQL
FEFGDKYRGK YDESIRVARN YYTSVSGYMD ELLWAGMWLY KATDNQRYLS YVVDNADTFG
GVGWSMTEFS WDVKFAGIQV LASQLLAEEK HMKHKDILKQ YQSKAEHYIC ACLNKNNGTK
NNVALTPGGL IYVRQWNNMQ HVSSGSFLTS VYSDLLTKSN RKYLKCHGGE VTPQELLQFS
KSQVDYILGS NPMNMSYLVG FGPRYPTRVH HRGASIVSYR ENKGFIGCTQ GYDSWYGSSD
PNPNVVVGAL VGGPNHNDEF NDRRGNYMQT EACTYNTAPL VGIFAKFSYL ENTVLHASSL
PLLREDGLLS FKPQVILGKL NNNEVMYALI IRFDLGRRMA MVGAYRHGSG VSLRCTTSLR
CFSTTGFREE RDTFGPIQVP NDKLWGAQTQ RSLQNFEIGG DRERMPEPII RSFGILKKCA
AKVNVEYGLD PSIGKAIMEA AQEVADGKLN DHFPLVVWQT GSGTQTNMNA NEVIANRAAE
ILGHKRGGKL VHPNDHVNRS QSSNDTFPTV MHIAAATEIN SRLVPNLKHL HTTLQAKTYE
FSDIVKIGRT HTQDATPLTL GQEFSGYATQ VKYGIDRVLC TLPRMYQLAQ GGTAVGTGLN
TKKGFDAKIA AAVADETRLP FVTAENKFEA LAAHDAFVET SGALNTIAVS LMKMANDIRF
LGSGPRCGFG ELILPENEPG SSIMPGKVNP TQCEALTMVC AQTIGNHVGL TVGGSNGHFE
LNVFKPMIAS SLLHSIRLIA DASASFEKNC VRGIQANRDR INKLLYESLM LVTSLNPKIG
YDNAAAVVKT AHKQGCTLKE AAVQLGVLTS EEFDQLVVPE KMIGPSD
//
