ID A9WBM5_CHLAA Unreviewed; 472 AA.
AC A9WBM5;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:ABY34832.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:ABY34832.1};
GN OrderedLocusNames=Caur_1614 {ECO:0000313|EMBL:ABY34832.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY34832.1, ECO:0000313|Proteomes:UP000002008};
RN [1] {ECO:0000313|Proteomes:UP000002008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC {ECO:0000313|Proteomes:UP000002008};
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY34832.1; -; Genomic_DNA.
DR RefSeq; WP_012257486.1; NC_010175.1.
DR RefSeq; YP_001635221.1; NC_010175.1.
DR AlphaFoldDB; A9WBM5; -.
DR STRING; 324602.Caur_1614; -.
DR EnsemblBacteria; ABY34832; ABY34832; Caur_1614.
DR KEGG; cau:Caur_1614; -.
DR PATRIC; fig|324602.8.peg.1849; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_0; -.
DR InParanoid; A9WBM5; -.
DR Proteomes; UP000002008; 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; 2.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
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 ECO:0000256|RuleBase:RU003427};
KW Oxidoreductase {ECO:0000313|EMBL:ABY34832.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002008}.
FT DOMAIN 10..84
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 209
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 210
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 472 AA; 50512 MW; B791A91DBCB6BBBC CRC64;
MSVGVAYTLT LRCQIENRPG MLGRLTTLIG EVGGDIGAID IVRAERNILV RDITVRVQDE
QHGEQLVAAI NTLQNIKVLQ VSDRVFLTHL GGKLATQSRV PLKTRDDLSL AYTPGVARVC
RAIADDPEKV YALTWKGNSV AVVSDGSAIL GLGNLGPEAA MPVMEGKAIL FKELANIDAV
PICLRSQDPD VIVQTVEQIA PSFGGINLED IAAPNCFIVE GRLEESLDMP VMHDDQHGTA
VVVLAALRNA VRIVGKRLAD VRVVVNGIGA AGTAIIRTLI EAGVGEITAV DRFGILVEGD
HARQTPMQRI IASQTNRERR RGDLAVALRG ADVFIGVSKG NILTPDHIRV MSSDPIVFAL
ANPIPEGDPD MLRQYARVVA TGRSDQPNQI NNVLSFPGIF RGALDVHARR ITSAMRLAAA
EALATVIPPE EMNEDYIVPS VFNRQVVPAI AAAVAQAAIA EGVARRTHMP GD
//
