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Database: UniProt
Entry: A0A0T5PFT1_9RHOB
LinkDB: A0A0T5PFT1_9RHOB
Original site: A0A0T5PFT1_9RHOB 
ID   A0A0T5PFT1_9RHOB        Unreviewed;       751 AA.
AC   A0A0T5PFT1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Malic enzyme {ECO:0000313|EMBL:KRS19884.1, ECO:0000313|EMBL:QEW29381.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:KRS19884.1, ECO:0000313|EMBL:QEW29381.1};
GN   Name=tme {ECO:0000313|EMBL:QEW29381.1};
GN   ORFNames=RIdsm_05225 {ECO:0000313|EMBL:QEW29381.1}, XM52_00240
GN   {ECO:0000313|EMBL:KRS19884.1};
OS   Roseovarius indicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS19884.1, ECO:0000313|Proteomes:UP000051401};
RN   [1] {ECO:0000313|EMBL:KRS19884.1, ECO:0000313|Proteomes:UP000051401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B108 {ECO:0000313|EMBL:KRS19884.1,
RC   ECO:0000313|Proteomes:UP000051401};
RA   Li G., Lai Q., Shao Z., Yan P.;
RT   "The draft genome sequence of Roseovarius indicus B108T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QEW29381.1, ECO:0000313|Proteomes:UP000325785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW29381.1,
RC   ECO:0000313|Proteomes:UP000325785};
RA   Vollmers J., Petersen J.;
RT   "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT   geographic distances.";
RL   Submitted (AUG-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}.
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DR   EMBL; LAXI01000001; KRS19884.1; -; Genomic_DNA.
DR   EMBL; CP031598; QEW29381.1; -; Genomic_DNA.
DR   RefSeq; WP_057813242.1; NZ_LAXI01000001.1.
DR   AlphaFoldDB; A0A0T5PFT1; -.
DR   STRING; 540747.SAMN04488031_102276; -.
DR   KEGG; rid:RIdsm_05225; -.
DR   PATRIC; fig|540747.5.peg.47; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000051401; Unassembled WGS sequence.
DR   Proteomes; UP000325785; Chromosome.
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; 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   ECO:0000313|EMBL:KRS19884.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051401}.
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;  81577 MW;  524AEC49916DC47A CRC64;
     MPNPKFSREE ALAFHLEPTP GKFEVTATVP MTTQRDLSLA YSPGVAVPCE EIARNPELAY
     DYTNKGNLVA VISNGTAVLG LGNLGALGSK PVMEGKAVLF KRFADVNSID IELDTEDPED
     FIKAVRLMGP TFGGINLEDI KAPECFIIEQ TLKEQMDIPV FHDDQHGTAV ICAAGLINAL
     HLSGKKIEDC RIVLNGAGAA GIACIELLKS MGARHENCIA CDTKGVIYQG RQDGMNQWKS
     AHAVSTELRT LEEAMKDADV FLGVSVKGAV TQDMVKSMAP DPVIFAMANP DPEITPEDAH
     EVRPDAIVAT GRSDYPNQVN NVLGFPYLFR GALDVHARAI NDEMKIACAH ALARLAREDV
     PDEVAIAYGR KLSFGRDYII PTPFDPRLIH TIPPAVARAC MDTGAARRPI VDMDAYELAL
     KSRLDPTASI MRSINARARN AQARMIFAEG DDPRVLRAAV QYTRTGFGHA VVVGRDEDVK
     QKLEAAGLGD AFDEIEITNA AKTEHLEEYK SFLYGKLQRR GFDQQDIHRL AARDRHVFSA
     LMLAHGHGDG LVTGATRKSA HVLDRINHVF DADAEHGAVG VTTLLHKGRI VMITDTLVHE
     WPDEEDLANI AERAADVARG LGIEPRVAFV SFSTFGYPRS ERAEKMHRAP MVLEARGVDF
     EFEGEMTVDV ALNKAAQDYY PFQRLTGPAN ILVVPARHSA SISTKLMQEM AGATVIGPIL
     AGIDKSIQIC SSTSTASDIL NMAVLAACKV G
//
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