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Database: UniProt
Entry: R4K1E8_CLOPA
LinkDB: R4K1E8_CLOPA
Original site: R4K1E8_CLOPA 
ID   R4K1E8_CLOPA            Unreviewed;       561 AA.
AC   R4K1E8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Malic enzyme {ECO:0000313|EMBL:AGK96922.1};
GN   ORFNames=Clopa_2033 {ECO:0000313|EMBL:AGK96922.1};
OS   Clostridium pasteurianum BC1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK96922.1, ECO:0000313|Proteomes:UP000013523};
RN   [1] {ECO:0000313|EMBL:AGK96922.1, ECO:0000313|Proteomes:UP000013523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC1 {ECO:0000313|EMBL:AGK96922.1,
RC   ECO:0000313|Proteomes:UP000013523};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA   Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT   "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL   Submitted (JAN-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   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
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DR   EMBL; CP003261; AGK96922.1; -; Genomic_DNA.
DR   RefSeq; WP_015615230.1; NC_021182.1.
DR   AlphaFoldDB; R4K1E8; -.
DR   STRING; 86416.Clopa_2033; -.
DR   KEGG; cpas:Clopa_2033; -.
DR   PATRIC; fig|86416.3.peg.2005; -.
DR   eggNOG; COG0281; Bacteria.
DR   HOGENOM; CLU_011405_5_2_9; -.
DR   OrthoDB; 3314528at2; -.
DR   Proteomes; UP000013523; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013523}.
FT   DOMAIN          81..262
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          272..529
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        104
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         247
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         248
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         271
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         417
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         461
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   561 AA;  62389 MW;  E855B97E4311DF74 CRC64;
     MSNISTDKKT VHTKLRGREL LNNPLLNKGT AFSKKERESL GLAGLLPSQV EDIEKQEDRC
     YKQFLSKPDN FSKHLYLMGL YDLNRTLFYK VVTSHIKEML PIIYTPTIGT GVKKYSEEFK
     SPLDSLYLSI DDKGNMEKAF DNLNEDDIEV MVITDSQGIL GIGDWGVNGV DISIGKLAVY
     TAAAGVDPSK VLPVVLDVGT DNKELLESEL YLGNRHVRVQ GKEYYDFIDQ FVKAALKKFP
     KVLIHWEDFG RENAHKVLEK YKDKILTFND DIQGTGAMIV SAVMSMSKAS NTLLKDQKIV
     IFGAGTAGIG IANQISSAME REGLSKEEAK NRFWCIDRYG LLIEDMDTLT DFQKPYARKR
     SEFGDFKDRN VELLDVVKIV KPTMLIGCSG VAGAFKEEVI REMAKGVENP AIMPISNPTS
     LAEAVPKDLI EWTEGKGLIV TGSPFEPVEY KGTTYKIGQA NNALLFPGLG FGAMIAKPRY
     VSEKMLEASS KAVAEFVDLS EKGAPLLPEV EMLHQVSQAV AVKVIEAALE EGINTVEIKD
     VKKVVSDETW YPEYYDIAPE D
//
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