ID A0A099BVS1_9BACT Unreviewed; 764 AA.
AC A0A099BVS1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KGI60182.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KGI60182.1};
GN ORFNames=HMPREF0671_07415 {ECO:0000313|EMBL:KGI60182.1};
OS Prevotella sp. S7 MS 2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1287488 {ECO:0000313|EMBL:KGI60182.1, ECO:0000313|Proteomes:UP000029732};
RN [1] {ECO:0000313|EMBL:KGI60182.1, ECO:0000313|Proteomes:UP000029732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7 MS 2 {ECO:0000313|EMBL:KGI60182.1,
RC ECO:0000313|Proteomes:UP000029732};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-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:KGI60182.1}.
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DR EMBL; JRPT01000035; KGI60182.1; -; Genomic_DNA.
DR RefSeq; WP_036898719.1; NZ_JRPT01000035.1.
DR AlphaFoldDB; A0A099BVS1; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR Proteomes; UP000029732; Unassembled WGS sequence.
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; 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:0000313|EMBL:KGI60182.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029732}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..400
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 76..83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 162
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 764 AA; 84147 MW; 07542A1112167AF9 CRC64;
MVKVTKEAAL LYHNNIRPGK IEVKPTKPYH TQTDLSLAYS PGVAYPCLEI QKNPDDVYKY
TDKGNLVAVI SNGTAVLGLG DIGAMSGKPV MEGKGLLFKI YGGIDVFDIE VDEKDPEKFC
EAIEKIAPSF GGINLEDIKA PECFYIEERL KKTLDIPVMH DDQHGTAIIS AAGLKNALEV
AGKNIGDVKI VVNGAGAAAI SCTKLYVALG AKVENILMLD SKGVITDNRE KLTPQKAMFA
TARRDVHTLE EAIKGADVFV GLSKGNILSQ DMIRSMAENP IVFALANPVP EISYEDAVAS
RPDVLMSTGR SDYPNQINNV IGFPYIFRGA LDVHAKAINE EMKLAAVEAI ANLAKQTVPD
VVNQVYHVTD LSFGPKYFIP KPVDPRLITE VSAAVAKAAI ESGVARKTIT DWDSYKQGLL
QLLGQETALT RKLHETARLH PQKVVFAEGG HPTMMKAAVQ AKQEGICFPI LLGNPDRLNR
LAQRLKLNLD GIEIIDMRAD QEQGRRATFA KHLAEKRARN GYTFEEAYDK MYERNYFGMS
LVEDGIADAF ITGLYTKYSN TIKVAKEVIG VREGYKTFGT MHILNTKKGI YYIADTLINR
HPDENVLTDI AKLSAHTVEF FNETPVMAML SYSNFGTDEV GSPVKVHMAV EQIQKEFPDL
AIDGEMQVNF ALNKELRDDK FPFSRLKGKD VNTLVFPNMS SANCSYKLLQ ALDADTEIIG
PIQMGLNKPI HFTDFESSVN DVVNITAVAV IDAYVEKLKK SNNQ
//
