ID J8Q2L7_SACAR Unreviewed; 671 AA.
AC J8Q2L7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=SU7_2019 {ECO:0000313|EMBL:EJS42896.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS42896.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS42896.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
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:EJS42896.1}.
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DR EMBL; ALIE01000128; EJS42896.1; -; Genomic_DNA.
DR AlphaFoldDB; J8Q2L7; -.
DR HOGENOM; CLU_011405_5_2_1; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000006968; Chromosome XI.
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 GO; GO:0008152; P:metabolic process; IEA:UniProt.
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:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 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:UP000006968}.
FT DOMAIN 166..347
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 357..611
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 34..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 332
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 333
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 356
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 501
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 541
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 671 AA; 74466 MW; B79D63B8529EB485 CRC64;
MLRTKLSVSI AARSQLARSL TASKTSTSLR RWSVQQQQRL YSSNTRPHKA TTTRENTFQK
PYSDEEVTKT PVGSRARKIF EAPQPHATRL TVGGAIECPL ESFQLLNSPL FNKGSAFTQE
EREAFNLEAL LPPQVNTLDE QLERSYKQLC YLKTPLAKND FMTSLRVQNK VLYFALIRKH
IKELVPIIYT PTEGDAIAAY SHRFRKPEGV FLDITEPDSV ERRLATYGGD KDVDYIVVSD
SEGILGIGDQ GIGGVRIAIS KLALMTLCGG VHPGRVLPVC LDVGTNNKKL ARDELYMGNK
FARIRGKQYD EFLDKFIKAV KKLYPSAVLH FEDFGVKNAR RLLEKYRYEL PSFNDDIQGT
GAVVMASLIA ALKHTNRDLK DIRVLVYGAG SAGLGIADQI VNHMVTHGVA KEDARKKIFL
MDRRGLILKS YEANSTPAQH GFAKDDADWT GINTRSLHDV VENVKPTCLV GCSTQASAFT
QDVVQEMHKH NPRPIIFPLS NPTRLHEAVP ADLMKWTDNN ALVATGSPFP PVDGYRISEN
NNCYSFPGIG LGAVLSRATT ITDKMISAAV DQLAELSPLR EGDSRPGLLP GLDTITNTSA
RLATAVILQA LEEGTARIEQ EQVPGGAPGE TVKVPRDFDE CLQWVKAQMW EPEYRPMIKV
QHDPSVHTNQ L
//
