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Database: UniProt
Entry: A0A1T5M4L4_9GAMM
LinkDB: A0A1T5M4L4_9GAMM
Original site: A0A1T5M4L4_9GAMM 
ID   A0A1T5M4L4_9GAMM        Unreviewed;       748 AA.
AC   A0A1T5M4L4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:SKC83083.1};
DE   Flags: Fragment;
GN   ORFNames=SAMN06296058_3636 {ECO:0000313|EMBL:SKC83083.1};
OS   Pseudoxanthomonas indica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=428993 {ECO:0000313|EMBL:SKC83083.1, ECO:0000313|Proteomes:UP000190341};
RN   [1] {ECO:0000313|EMBL:SKC83083.1, ECO:0000313|Proteomes:UP000190341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P15 {ECO:0000313|EMBL:SKC83083.1,
RC   ECO:0000313|Proteomes:UP000190341};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC       family. {ECO:0000256|ARBA:ARBA00007686}.
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DR   EMBL; FUZV01000003; SKC83083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5M4L4; -.
DR   STRING; 428993.SAMN06296058_3636; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000190341; 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; 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.
PE   3: Inferred from homology;
KW   Metal-binding {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:UP000190341}.
FT   DOMAIN          13..146
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          158..393
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        89
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         71..78
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         131
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         132
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         157
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         281
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:SKC83083.1"
FT   NON_TER         748
FT                   /evidence="ECO:0000313|EMBL:SKC83083.1"
SQ   SEQUENCE   748 AA;  80867 MW;  42FFA2D369D3A80B CRC64;
     KQAALEYHRL SPPGKIKVTP TKPMLTQRDL ALAYSPGVAY ACEAIVEDPK AASELTARGN
     LVAVVTNGTA VLGLGNIGAL AGKPVMEGKG VLFQKFAGID VFDIEIDETD PDKLVDIIAS
     LEPTFGGINL EDIKAPECFI VERKLRERMR IPVFHDDQHG TAIIVGAAVV NALEVVGKRI
     EDVKLATSGA GAAGIACLDM LVALGLKPEN ILAFDREGVI YSGRAHLDPD KARYARETDK
     RTLAEIVAGA DIFLGLSAGG ILKPEMVATM AAKPIILALA NPNPEILPAD AKAVRPDAII
     GTGRSDYPNQ VNNALCFPYI FRGALDVGAT VINEAMKVAC VHAIAHLARR EASDLGTAYG
     DDVPCFGPEY LIPRPFDPRL LVEVAAAVAQ AAMDSGVALR PIQDMRGYRE KLGQFVYRTS
     LMMKPVYDRA KADKKRVVYA EGEEETVLRA VQTVIDEGLA HPILIGRPDV IAARIERLSL
     RMRAGVDFEL TNQDDDPRFN DYWQHYHALT SRRGVTPAAA KNLMRSRPTL IAAVMVARGE
     ADAMVSGIVG RFHKKLGYVR SVIPLEPGVQ STSAMTGVIN NQGAYFFLDT HVQDDPTAEQ
     IAEATLQAAY RLKLFGIEPR VALLSHSNFG SHETPGALKM RKVRELLLKR MPKLNVDGEM
     QGDTAWDEVL RNRIMPGSTL TGRANLFVLP NLDAANIAYN MVRVVTDGVA IGPILMGISK
     PVHILTTSAT PRRVVNMTAI AAVDAQIR
//
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