ID A0A0B1ZK85_9SPHN Unreviewed; 753 AA.
AC A0A0B1ZK85;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KHK89571.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KHK89571.1};
GN ORFNames=LK12_21030 {ECO:0000313|EMBL:KHK89571.1};
OS Novosphingobium malaysiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1348853 {ECO:0000313|EMBL:KHK89571.1, ECO:0000313|Proteomes:UP000031057};
RN [1] {ECO:0000313|EMBL:KHK89571.1, ECO:0000313|Proteomes:UP000031057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 273 {ECO:0000313|EMBL:KHK89571.1,
RC ECO:0000313|Proteomes:UP000031057};
RA Lee L.-H.;
RT "Genome sequence of Novosphingobium malaysiense MUSC 273(T).";
RL Submitted (OCT-2014) 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:KHK89571.1}.
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DR EMBL; JTDI01000007; KHK89571.1; -; Genomic_DNA.
DR RefSeq; WP_039288613.1; NZ_JTDI01000007.1.
DR AlphaFoldDB; A0A0B1ZK85; -.
DR STRING; 1348853.LK12_21030; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000031057; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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: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; 2.
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 ECO:0000313|EMBL:KHK89571.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031057}.
FT DOMAIN 23..156
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 168..403
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 291
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 753 AA; 81433 MW; FBA8AA5A8504061C CRC64;
MSEKSKVQFT EREALFYHET IRPGKIEIIA SKPMATQRDL SLAYSPGVAV PVQAIADDPQ
KAYDYTAKGN LVAVISNGTA ILGMGNLGAL ASKPVMEGKA VLFKRFADVD SIDIELASEN
VDELIEAIAM MEPSFGGINL EDIKAPECFI IEQTLRERMN IPVMHDDQHG TAIIAAAGLI
NAAHLTGRDL DKLKVVVNGA GASALACTAL IKSMGVRNDN VIVCDSKGVI YKGRENVDQF
KSAHAVDTDR RTLTEALKGA DVFLGLSVAG AVTQEMVKEM ADEPIIFAMA NPDPEITPPA
VKAVRPDAIV ATGRSDYPNQ VNNVLGFPFI FRGALDVRAT AINEEMKIAA ARAIAELARE
QVPEEVAAAY GETQQFGREY IIPAPFDPRL MEVVPMAVAK AAMESGVAQK HIDDFDAYRH
ELKGRLNPTT SVLSSVYAQV KANPKRVIFA EADNEVVLRA AIQFRDFGYG EPVLVGRTKN
IHNLMNELGV ADPDSYRIEN SMVSEHVSPM VEMLYERLKR RGFLQRDVQR MCNTDRNVFA
AGLLKLGVGD AMITGMTRPF AQSMKEVRRV LDPAENKLPF GIHMLVGKNH TVFLADTTIN
ERPNADELAV IATETAAVAR RLGHEPRVAF LSYSTFGNPS GKWLDTIRGA VQILEGQDPG
FEFDGDMAPD AALNPKIMAL YPFCRLSAPA NVLIMPGLQS ANISAKLLRE IGGATNIGPM
LLGMEKPVQI VPMTAIAPDV LTSAVLAAAG VTG
//
