ID A0A2T6KLT2_9RHOB Unreviewed; 751 AA.
AC A0A2T6KLT2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:PUB17166.1};
GN ORFNames=C8N45_102176 {ECO:0000313|EMBL:PUB17166.1};
OS Yoonia sediminilitoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=1286148 {ECO:0000313|EMBL:PUB17166.1, ECO:0000313|Proteomes:UP000244523};
RN [1] {ECO:0000313|EMBL:PUB17166.1, ECO:0000313|Proteomes:UP000244523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29955 {ECO:0000313|EMBL:PUB17166.1,
RC ECO:0000313|Proteomes:UP000244523};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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}.
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:PUB17166.1}.
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DR EMBL; QBUD01000002; PUB17166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6KLT2; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000244523; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000244523}.
FT DOMAIN 20..153
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 165..401
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 78..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 164
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 289
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 751 AA; 81212 MW; FB4003DA086A32F2 CRC64;
MAKNKLTRED ALQFHMQPSP GKWEIQATVP MTTQRDLSLA YSPGVAIPCE EIARDPATAY
DYTNKGNLVA VISNGTAVLG LGNLGALGSK PVMEGKSVLF KRFADVNSID IELDTEDPDE
FIKAVRLMGP TFGGINLEDI KAPECFIIEQ TLKEQMDIPV FHDDQHGTAV ICAAGLLNAL
HLSGKKIEDV KIVLNGAGAA GIACLELLKA MGAKHDNCIM CDTKGVIYQG RTDGMNQWKS
AHAANTRARS LDDAMKDCDV FLGVSAKGAV TQEMVSNMAK NPVIFAMANP DPEITPEDAH
AVREDAIVAT GRSDYPNQVN NVLGFPYLFR GALDIHARAI NDEMKIACAE ALAALAREDV
PDEVALAYGK KLSFGRDYII PTPFDPRLIH RIPTAVAQAG MKTGVARRPI VDMDAYEQSL
KSRMDPTQSM LRSLNARARA AQSTVIFAEG DDPRVLRAAV LYQRSGMGKA LVVGREDDVK
EKLTAEGLGE AVGELTIVNA ANTEYLETYK NFLYKRLQRK GFDVADVHRL AARDRHVFAS
LMLAHGHADG MVTGATRKSA HVLELINHVF DAQPHDGAVG VTAVLHKGRI VLITDTLVHE
WPDENDLADI AERGASVARD LGLDPRVAFL SFSTFGYPVS ERAEKMHQAP KVLDTRGVDF
EYEGEMTVDV ALNTQAQEHY PFSRLTGPAN VLVVPARHSA SISVKLMQEM AGATVIGPIL
SGIGKPVQIC STVSTVNDIL NMAVIAACGV D
//
