ID A0A0H5SCT2_BRUMA Unreviewed; 589 AA.
AC A0A0H5SCT2; A0A0K0IVR9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN Name=bma-men-1.1 {ECO:0000313|WormBase:Bm12784};
GN ORFNames=Bm12784 {ECO:0000313|EMBL:CRZ26426.1,
GN ECO:0000313|WormBase:Bm12784}, BM_Bm12784
GN {ECO:0000313|EMBL:CRZ26426.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CRZ26426.1};
RN [1] {ECO:0000313|EMBL:CRZ26426.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ26426.1};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CRZ26426.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ26426.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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; LN857023; CRZ26426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5SCT2; -.
DR WormBase; Bm12784; BM45645; WBGene00233045; Bma-men-1.1.
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}.
FT DOMAIN 92..272
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 282..533
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 257
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 258
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 281
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 464
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 589 AA; 66176 MW; 377B4944FA8D1992 CRC64;
MANNSILEDL PEVKQLYRHE IAFPAYRGAD LLRVPRYNKG MAFSLSERQH LGIHGLLPAA
FETEELQVYR VICQLREEND NLKKYIILDN LQDQNEKLYY RVVIEHVQEL LPIIYTPTVG
LACQKFGHIF RRPKGIYITI NDNSISKIYQ ILSNWPEHDV RAIVVTDGER ILGLGDLGAY
GMGIPIGKLS LYVAFGGVQP KWCLPIVLDC GTDSEINPFY TGLRQKRVRG AQYDLLIDNF
MKACVKRFGQ KTLIQFEDFA NTNAGRLLAK YRNEYATFND DIQGTASIVV AGLLSCGNIL
QRKMSDQILL FLGAGAAATG TADMCVLQMQ REGTSEKDAC KRIFLINSKG LITVNSPVVK
SEHQKYAKEM AHMKDLLEII EKVRPTGIIG VSTVHGAFSE QIIRKMVEIN ERPIIFALSN
PTSKSECTAE EAIQYTKGKA LFASGSPFPD VNYDGKCYKP GQGNNSYIFP GIGLGVVLFE
VRHIDEEIFL IAAREVASSV TEEDISFGCI YPSLCKIREI SVAIALEIGK YSYKHGIAGL
YPQPENMEQY IRSQIYSVNY DELIYKQYNW PVEDTIKSIP VLPAKENNS
//
