ID B0T685_CAUSK Unreviewed; 762 AA.
AC B0T685;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+)), Phosphate acetyltransferase {ECO:0000313|EMBL:ABZ74088.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ABZ74088.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:ABZ74088.1};
GN OrderedLocusNames=Caul_4968 {ECO:0000313|EMBL:ABZ74088.1};
OS Caulobacter sp. (strain K31).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ74088.1};
RN [1] {ECO:0000313|EMBL:ABZ74088.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31 {ECO:0000313|EMBL:ABZ74088.1};
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., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; CP000927; ABZ74088.1; -; Genomic_DNA.
DR AlphaFoldDB; B0T685; -.
DR STRING; 366602.Caul_4968; -.
DR KEGG; cak:Caul_4968; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) 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 GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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; IPR045213; Malic_NAD-bd_bact_type.
DR InterPro; IPR012188; ME_PTA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF036684; ME_PTA; 1.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:ABZ74088.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036684-2};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABZ74088.1}; Transferase {ECO:0000313|EMBL:ABZ74088.1}.
FT DOMAIN 23..156
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 168..405
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 81..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 167
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 292
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 762 AA; 81980 MW; 521EBD5A6472B360 CRC64;
MSDAEKKTFT DEEALNFHRY PTPGKIAIVP TKPMATQRDL SLAYSPGVAV PVHAIAADPD
MAYEYTSKGN LVAVISNGTA ILGLGDLGAL ASKPVMEGKS VLFKRFGDVD SIDIEISSKD
ADEIITVVKN IGITFGGINL EDIKSPECFR IETELQELLD IPVFHDDQHG TAIICAAGLI
NACHITGKKL EDVRVVLNGP GAAGIASLEL IKAMGVRPEN CIAVDSKGVL YQGRTEGMNQ
WKSAHAVDTP LRTLAEAAKG ADVLLGLSAK GAFTPEIIAS MAPNPVIFAM ANPDPEITPE
EVHAVRKDAI MGTGRSDYPN QVNNVLGFPY IFRGALDVRA RRVNHEMKIA CANALAMLAR
EDVPDEVAAA YHGRQLKFGP QYIIPSAFDP RLIWYVPPFV AQAAMDTGVA RKPIADMDAY
RASLAQRLDP TAGFLQKISG AVLANPKRIV FAEGEDPTVI RAAYAYQTGG FGKAILCGRE
NLVHENMRVV GLDPETAGLE IVNARLSDRN PDYVDALYAR LQRQGYLKRD VQRLINQDRN
SFAASMVTLG EADGMVTGVT RSFDQALEEV LRVVDPAPGG RIMGMSVVLA KGRTIFVADT
NVTELPEAEE LVEIACEAAR AVTRLGFKPR VAFMSYSTFG NPMGLRSEKV REAVAMLDEM
DVDFEYEGEM PPELALDPER RANYPFMRLT DSANILIMPA IHAASISTKL VQSLGGATVI
GPVLLGLSKP IQIAPLSASV SKILNMAMMA AYEGAGDLGA AE
//
