ID A0A016UBT0_9BILA Unreviewed; 665 AA.
AC A0A016UBT0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN Name=Acey_s0048.g1717 {ECO:0000313|EMBL:EYC12302.1};
GN ORFNames=Y032_0048g1717 {ECO:0000313|EMBL:EYC12302.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC12302.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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 -!- 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:EYC12302.1}.
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DR EMBL; JARK01001384; EYC12302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016UBT0; -.
DR STRING; 53326.A0A016UBT0; -.
DR Proteomes; UP000024635; 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; 2.
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; 2.
DR PIRSF; PIRSF000106; ME; 2.
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:UP000024635}.
FT DOMAIN 138..321
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 331..606
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 234
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 306
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 307
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 330
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 536
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 665 AA; 74869 MW; 358511AFC7CAA174 CRC64;
MAREYAQPSL FEIEKCTRKK GKNEMLRTLQ QQSSRSLSTT TLLRDGPEID LSDPKQLALH
KLYRPERITP LKRGLELLKT PSLNKGMAFS LYERQYLGIH GLLPPAFMTS EQQAYRVMTK
LREQPNDLAK YIQLDSLQDR NEKLFYRVLC DNIKELMPIV YTPTVGQACQ KFGFIYRNPK
GLYITINDNS ISKIYQILAN WPSTNIKAIV VTDGERILGL GDLGAYGIGI PVGKLALYVA
LAGLFPEWCL PVLIDVGTDN QALLNDPFYT GLRRTRVRGP EYDTLIDNFM KACTKRFGRD
TLIQFEDFGN QNAYRLLDRY KNEYCMFNDD IQGTASVVVA GLLATTRITK KRLSQQKLVF
LGAGGHDIMV TKYKTVLYVF LNFVMNQAAT GVAEMCVRQM VDEGLTEKEA CANIFMMDID
GLITKSRSAT LSDRHLRFAK DLPDTKSLLE VVRTVKPGGL IGASTVSGAF TEEIIQEMAN
INPRPIIFAL SNPTSKAECT AEAAFRITNG TVLFASGSPF DNVELNGKLY KPGQGNNAYI
FPGIALGCVL FKAKHIPDKL FLLAARRVAD SVTEKSLTTF SRLYPRLKSI RELSIQIAIE
VGNYLYSHNL ATLHPKPEDM ELFIRQHVYS VEYTDLINKT YDWPAKDAKH GFPVPVLRRS
SMDDE
//
