ID U6JA97_ECHGR Unreviewed; 583 AA.
AC U6JA97;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN Name=EGR_02017 {ECO:0000313|WBParaSite:EgrG_000645800};
GN ORFNames=EGR_02017 {ECO:0000313|EMBL:EUB63213.1}, EgrG_000645800
GN {ECO:0000313|EMBL:CDS18660.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB63213.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB63213.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
RN [2] {ECO:0000313|EMBL:CDS18660.1, ECO:0000313|Proteomes:UP000492820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [3] {ECO:0000313|EMBL:CDS18660.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|WBParaSite:EgrG_000645800}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (OCT-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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; LK028578; CDS18660.1; -; Genomic_DNA.
DR EMBL; APAU02000008; EUB63213.1; -; Genomic_DNA.
DR AlphaFoldDB; U6JA97; -.
DR STRING; 6210.U6JA97; -.
DR EnsemblMetazoa; XM_024491266.1; XP_024354409.1; GeneID_36337732.
DR WBParaSite; EgrG_000645800; EgrG_000645800; EgrG_000645800.
DR OMA; QIVNHMV; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR Proteomes; UP000492820; Unassembled WGS sequence.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF90; MALIC ENZYME-RELATED; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149}.
FT DOMAIN 87..268
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 278..536
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 253
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 254
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 277
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 583 AA; 65185 MW; 851A1C8E2D914A36 CRC64;
MMRRSLVQFI ARRCFASEIH SYGVGVLRNP VTNKGTAFTI RERQLLGIHG LLPPAVSNLD
VQSRKMINNL KHLEDNLQRY IFLIGLQDRN ETLFYKVVTE HTEYCMPLIY TPTVGLACQK
YGLVFRRPRG LYITIHDRYN IDDILKNWPE PIVRTIVVTD GERILGLGDL GAYGMGIPVG
KLSLYSALAG VNPRHCLPIV LDVGSDNQDL LNDMHYLGIK HKRIRDARYD ELLDNFMRAI
VRRYGNNCLV QFEDFGNRNA FRILERYRHD YCTFNDDIQG TASVTVAGLI AAGRLTGRRL
SDDTYLFVGA GEAASGIAHL LKTAMVMHGL PEADAINKIY MFDKDGLLVE GRPEGNIDEH
NSTFVRTDVE PMRNLEEIVR KLKPTALIGA SGVGGLFTHR ILQQMKKNVD RPIIFALSNP
TDKAECTAEA AYNTTGGACV FASGSPFGEV TMNVGGQVKT FKPGQCNNSY IFPGVGLAIT
ACKLRPIPDE CFAVAADCLA EQVKEEDLAL GRVFPPLSQI RPVSLAIAHR VAEFAYEEDV
AHLIPKPENL VAYIQDQMYV PKYDSALPDF YDWPEEAIRK PLE
//