ID A7NM15_ROSCS Unreviewed; 473 AA.
AC A7NM15;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:ABU58570.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:ABU58570.1};
GN OrderedLocusNames=Rcas_2490 {ECO:0000313|EMBL:ABU58570.1};
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372 {ECO:0000313|EMBL:ABU58570.1, ECO:0000313|Proteomes:UP000000263};
RN [1] {ECO:0000313|EMBL:ABU58570.1, ECO:0000313|Proteomes:UP000000263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8 {ECO:0000313|Proteomes:UP000000263};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-2007) 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}.
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DR EMBL; CP000804; ABU58570.1; -; Genomic_DNA.
DR RefSeq; WP_012120994.1; NC_009767.1.
DR AlphaFoldDB; A7NM15; -.
DR STRING; 383372.Rcas_2490; -.
DR KEGG; rca:Rcas_2490; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_0; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000000263; Chromosome.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR CDD; cd04887; ACT_MalLac-Enz; 1.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.30.70.260; -; 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; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
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; IPR045213; Malic_NAD-bd_bact_type.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000313|EMBL:ABU58570.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000263}.
FT DOMAIN 13..87
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 213
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 238
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 473 AA; 50267 MW; 642C7B339FB76732 CRC64;
MTGTNQGIAY TLTIRCQIDN RPGMLGTIAT AIGENGGNIG AIDIVRVDRK HIVRDITVRV
QDELHGDRIV RRINALPGVV VTNVSDRVFS LHQGGKISIQ SRTPLKSRDD LSLIYTPGVA
RVCRAISRDE ENAFSLTIKK NSLAVVSDGS AVLGLGNLGA AAAIPVMEGK AVLFKELADI
DAFPICLKSQ DPDVIVATVE QISPVFGAIN LEDIAAPKCF DIEERLAERL DIPVMHDDQH
GTAVVVLAGL RNAATLVGKR LDQMRVVVNG VGAAGTAIIH NLLIAGVGEV TAVDRTGILN
IDEDQHLTPM QRQIAARTNR ERRRGGLAEA LVGADAFIGV STGNLLTAGM VQSMGSDPIV
FALANPIPEG DPEMLQHYAR VVATGRSDFP NQINNVLSFP GIFRGALNVR AAKITPRMRL
AAAEGLASVI SHEELSEEYI IPSVFNRDIV PAVAAAVARA AREEGVARAD NGA
//
