ID A0A0T6AK58_9BACT Unreviewed; 475 AA.
AC A0A0T6AK58;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Malate dehydrogenase, malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:KRT75457.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:KRT75457.1};
GN ORFNames=XU13_C0001G0032 {ECO:0000313|EMBL:KRT75457.1};
OS Candidatus Rokubacteria bacterium CSP1-6.
OC Bacteria; Candidatus Rokubacteria.
OX NCBI_TaxID=1640509 {ECO:0000313|EMBL:KRT75457.1, ECO:0000313|Proteomes:UP000051916};
RN [1] {ECO:0000313|EMBL:KRT75457.1, ECO:0000313|Proteomes:UP000051916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-6 {ECO:0000313|EMBL:KRT75457.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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 -!- 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:RU003427}.
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:KRT75457.1}.
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DR EMBL; LDXP01000001; KRT75457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6AK58; -.
DR STRING; 1640509.XU13_C0001G0032; -.
DR PATRIC; fig|1640509.3.peg.33; -.
DR Proteomes; UP000051916; Unassembled WGS sequence.
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; 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; 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 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.
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:0000313|EMBL:KRT75457.1}.
FT DOMAIN 12..86
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 237
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 475 AA; 50972 MW; 95AC9FB783AB7309 CRC64;
MIGAPSASYS MTVRLDIVNR PGMLGKVTSA IGKAGGDIGA IDLVQVGRNT VTRDITFKAR
DDKHGTQVVD RLRAVSGVKV VNVSDRTFLM HLGGKIEVRG KMAVKTRDDL SMAYTPGVAR
VCMAIHEDPE KAYTLTIKQN CVAVVTDGTA VLGLGDIGPR AALPVMEGKA LLFKELAGVD
AFPICLATKD PNEIVKIVKA ISPVFGGINL EDISAPRCFT IEERLKKELD IPVFHDDQHG
TAVVVLAALI NAFKIVKKRM SDVTVVFSGA GASATATAKL LMKVGVRHVI GADRSGILYK
GRKENMNPMK VWFAEHTNPK RLRGEIGQAL EGADVFIGLS GPGVVTLKDI KRMARDPIVF
AMANPVPEIM PEEAGRHVKV MATGRSDYPN QINNVCGFPG IFRGLLDVRA RTVNDEMKIS
AAHAIANIVS KSELNAEYIT PSVFDKRVVE AVASAVAQAA YDTGVARRKR KVVSA
//
