ID V6F5Z0_MAGGM Unreviewed; 762 AA.
AC V6F5Z0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:CDL00849.1};
DE EC=1.1.1.39 {ECO:0000313|EMBL:CDL00849.1};
GN Name=dme {ECO:0000313|EMBL:CDL00849.1};
GN OrderedLocusNames=MGMSRv2__3634 {ECO:0000313|EMBL:CDL00849.1};
OS Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS / MSR-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=431944 {ECO:0000313|EMBL:CDL00849.1, ECO:0000313|Proteomes:UP000018922};
RN [1] {ECO:0000313|EMBL:CDL00849.1, ECO:0000313|Proteomes:UP000018922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1
RC {ECO:0000313|Proteomes:UP000018922};
RX PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA Wang L., Li J.;
RT "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL Genome Announc. 2:e00171-e00114(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG794546; CDL00849.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F5Z0; -.
DR STRING; 1430440.MGMSRv2__3634; -.
DR KEGG; mgy:MGMSRv2__3634; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR Proteomes; UP000018922; Chromosome I.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) 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: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 ECO:0000313|EMBL:CDL00849.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018922}.
FT DOMAIN 20..153
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 165..402
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 762 AA; 83202 MW; AB54EB6A49C170A7 CRC64;
MSISDELRDS ALEYHRLPTP GKISVTPTKP LGNQRDLALA YSPGVAAACE EIVRDPEAVS
EMTARGNLVA VVTNGTAVLG LGNIGPLAAK PVMEGKGVLF KKFAGIDVFD MEIAENDADK
LVDIIASMEP TFGAINLEDI KAPECFEVER KLKERMSIPV MHDDQHGTAI VVGAAMVNAL
RIVGKDIGKV RLVASGAGAA ALACLNLLVS LGVKRENIWV TDIKGVVYKG RNELMDPYKE
IFAQETDART LDDVIGGADI FLGLSAPRVL TGDMVAKMAD QPIVFALANP TPEILPDEVK
AARKDAIIAT GRSDYPNQVN NVLVFPYIFR GALDVGATQI NEEMKLAATY ALAELAMAES
DERVRAAYGE QRLSFGPEYL IPKPFDSRLI LKIAPAVARA AMSSGVARRP IIDFQAYLER
LSQWVFRSGL VMKPVFDRAK QDVRRVVYCE GEGRRVLLAV QAVVDEGVAF PVLIGRRDVV
VKRIKDLDLR LTIDEDFELC DPQDDPRYND YWRNYHTLLE RKGVSPDYAR TVVRTRSTVI
GTLMVRRREA DAMICGTIGR YDKHLEHITD VIGVRDTVKV PAAMNLLIMP QGTFFICDTY
VTADPSPEQI VENTLLAAEE VRRFGIEPKV AFLSHSNFGA RDTASAQKMR AAIALLHERA
PYLEAEGEMH GDAALEESIR SRIFPNSRLK GQANLLIMPN LDAANISFNL LKVLGEGLSV
GPILMGAALP AHILTPSATV RNIVNMTALA AVDAQMAAHQ RG
//
