ID M9RBM7_9RHOB Unreviewed; 770 AA.
AC M9RBM7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=NAD-dependent malic enzyme Dme {ECO:0000313|EMBL:AGI69168.1};
DE EC=1.1.1.39 {ECO:0000313|EMBL:AGI69168.1};
GN Name=dme {ECO:0000313|EMBL:AGI69168.1};
GN ORFNames=OAN307_c37090 {ECO:0000313|EMBL:AGI69168.1};
OS Octadecabacter antarcticus 307.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI69168.1, ECO:0000313|Proteomes:UP000005307};
RN [1] {ECO:0000313|EMBL:AGI69168.1, ECO:0000313|Proteomes:UP000005307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=307 {ECO:0000313|EMBL:AGI69168.1,
RC ECO:0000313|Proteomes:UP000005307};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
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; CP003740; AGI69168.1; -; Genomic_DNA.
DR RefSeq; WP_015501119.1; NC_020911.1.
DR AlphaFoldDB; M9RBM7; -.
DR STRING; 391626.OAN307_c37090; -.
DR KEGG; oat:OAN307_c37090; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR Proteomes; UP000005307; Chromosome.
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:AGI69168.1}.
FT DOMAIN 36..169
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 181..418
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 112
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 94..101
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 155
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 180
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 305
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 770 AA; 82462 MW; 63610D0E17E605F0 CRC64;
MPETPPKTPN DTSAIDAQKK ENLRQAALDY HRYPKPGKLE IRATKPMANG RDLARAYSPG
VAEACLEIKN NPAAAQDYTA RGNLVAVVTN GSAVLGLGNI GALASKPVME GKAVLFKKFA
NIDCFDIELN EPDPKKLADI VCALEPTFGA INLEDIKAPE CFIVEKICRE RMNIPVFHDD
QHGTAIVVGA AATNALAVSG KKFEDIKIVS TGGGAAGIAC LNMLLKLGVK RENVWLCDIE
GLVYEGRETD MTPQKAEFAQ GKTAATLGDV IDGADMFLGL SGPGVLKPDM VARMTKAPII
FALANPNPEI SPEDARAVAP DAIMATGRSD FPNQVNNVLC FPFIFRGALD VGATEINDAM
KIGCVEGIAA LARATTSAEA AAAYQGEQMT FGPDYLIPKP FDPRLMGVVA SAVAKAAMET
GVATKQVDLP SYKAGLDASV FKSAMLMRPV FEAAAKEARR IVFTEGEDER VLRAAQAVLE
ETTETPILIG RPDVIALRAE RAGLDIDISS LDIVNPENDP RYRDYWETYH TLMSRNGVTP
DLAKAVMRTN TTAIGAVMVQ RGEADSMICG TFGQFRWHLN YIEQVLGKDH KVQGALSMMI
LEDGPLFIAD THVRSEPTPE QIAQTAIGAA RHVKRFGLKP NVAFCAQSQF GNLDCDTGNR
IRAAMSILAA QKVDFTYEGE MNVDAALDPE LRERLLPCGR MKGAANVLIF GHADAASGVR
NILKMKAGGL EVGPILMGMG NRAHIVTPSI TPRGLLNMAA IAGTPVKVYG
//
