ID W4S625_9XANT Unreviewed; 769 AA.
AC W4S625;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:GAE52065.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:GAE52065.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:GAE52065.1};
GN ORFNames=XPU_3597 {ECO:0000313|EMBL:GAE52065.1};
OS Xanthomonas arboricola pv. pruni str. MAFF 311562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1414836 {ECO:0000313|EMBL:GAE52065.1, ECO:0000313|Proteomes:UP000019143};
RN [1] {ECO:0000313|EMBL:GAE52065.1, ECO:0000313|Proteomes:UP000019143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311562 {ECO:0000313|Proteomes:UP000019143};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) 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}.
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:GAE52065.1}.
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DR EMBL; BAVB01000330; GAE52065.1; -; Genomic_DNA.
DR AlphaFoldDB; W4S625; -.
DR Proteomes; UP000019143; Unassembled WGS sequence.
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; 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 Acyltransferase {ECO:0000313|EMBL:GAE52065.1};
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 ECO:0000313|EMBL:GAE52065.1}; Transferase {ECO:0000313|EMBL:GAE52065.1}.
FT DOMAIN 19..152
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 164..399
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 77..84
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 163
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 287
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 769 AA; 83860 MW; 2BA77D8AE207A94F CRC64;
MSNDDFKQAA LDYHRQQPAG KIKVTATKPM LTQRDLSLAY SPGVAFACEA IVEEPTQASE
LTARGNLVAV ITNGTAVLGL GNIGPLASKP VMEGKGVLFQ KFAGIDVFDI EINENDPDKL
VDIIASLEPT FGGINLEDIK APECFIVERK LRERMNIPVF HDDQHGTAII VGAAVLNALV
VTGKKIEEVK LATTGMGAAG ISCVNMLVSL GLKPENILAL DRDGVIHTGR TDLDPDKQRY
ARDTDKRTLA EIVEGADIFL GLSAAGILKP EMVASMARQP VIFALANPNP EITPEAAKAV
RPDCIIGTGR SDYPNQINNV LCFPYLFRGA LDVGATGINE EMKIACVKAI AAMARREASD
LGAAYGGETP SFGPEYLIPR PLDPRLLVEL SSAVAQAAMD SGVATRPITD MEAYRDKLGQ
FVYRTSLMMK PVYDRARADK QRVVYAEGEE EVVLRAVQNV VDEGLAFPIL IGRPDVIEAR
IERMGLRLTA GVDFEITNIL DDPRFNEYWQ YYHALTERRG VTVTAAKELM RSRPTLIAAV
MVARGEADAM LSGVVGRFHK KLGYARSVIP LEPRVSSTSA MTGVINQLGV FFFLDTHVQE
DPTVEQVVEA TLQAAYRLKL FGIEPNIALL SHSNFGSHDS RDALKMRQVR EALLKRKPEL
NIDGEMQGDT AWDEALRKQI MPNSTLKGRA NLFVLPNLEA ANIAYNLVRV FTDGVAIGPI
LMGISKPVHI LTTSATSRRV MNMTAIAAVD AQIRRQRDAE KNASEKNSD
//
