ID I0TFG1_9BACT Unreviewed; 762 AA.
AC I0TFG1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Malic enzyme, N-terminal domain / malic enzyme, NAD-binding domain / phosphate acetyl/butyryl transferase multi-domain protein {ECO:0000313|EMBL:EID34364.1};
GN ORFNames=HMPREF9969_1264 {ECO:0000313|EMBL:EID34364.1};
OS Prevotella sp. oral taxon 306 str. F0472.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1095752 {ECO:0000313|EMBL:EID34364.1, ECO:0000313|Proteomes:UP000004421};
RN [1] {ECO:0000313|EMBL:EID34364.1, ECO:0000313|Proteomes:UP000004421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0472 {ECO:0000313|EMBL:EID34364.1,
RC ECO:0000313|Proteomes:UP000004421};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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:EID34364.1}.
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DR EMBL; AJIN01000011; EID34364.1; -; Genomic_DNA.
DR RefSeq; WP_009434140.1; NZ_AJIN01000011.1.
DR AlphaFoldDB; I0TFG1; -.
DR STRING; 1095752.HMPREF9969_1264; -.
DR PATRIC; fig|1095752.3.peg.314; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000004421; 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 Transferase {ECO:0000313|EMBL:EID34364.1}.
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 762 AA; 83779 MW; 2F1365CF75506C2D CRC64;
MVKVTKEVAL EYHHNGRPGK IEVKPTKPYS TQTDLSLAYS PGVAYPCLEI QQNPDDVYKY
TTKGNLVAVI SNGTAVLGLG NIGAMSGKPV MEGKGLLFKI YGGVDVFDIE VNEQDPDKFC
EAVEKIAPTF GGINLEDIKA PECFAIEERL KRTLDIPVMH DDQHGTAIIS AAGLKNALEV
AGKDISKIKL VVNGAGAAAI SCTKMYVALG VKKENIVMLD SKGVITSDRE NLTPQKALFA
TDRRDVHTLE EAINGADVFV GLSKGNILSQ DMIRSMNEKP IVFALANPVP EISYDDAIAA
RPDVIMSTGR SDYPNQINNV IGFPYIFRGA LDVHAKAINE EMKMAAVHAI ADLAKQTVPD
VVNEVYHVND LTFGPKYFIP KPVDPRLITE VSAAVAKAAM DSGVARTPIK DFEAYKQHLR
QMLGQETKLT RSLHATAAQH PQRIVFAEGG HPTMMKAAVQ AKQEGICVPI LLGNQDRLNR
VANRLKLDIS DIEIIDMRAD KEQGHRATYA KHLAEKRARE GYTFEEAYDK MYERNYYGMS
MVENGDADAF ITGLYTKYSN TIKVAKEVIG IRPEYKHFGT MHILNTKKGV FYIADTLINR
HPDSDVLTDV ARLAAHSVKF FNDEPAIAML SFSNFGSDNG GSPEQVREAV AKLQAECPDL
AIDGEMQVNF ALNKELRDEK FPFTRLKGKD VNTLVFPDLS SANSGYKLLQ ALSPEAEVIG
PIQMGLNKPI HFTDFESSVR DIVNITAVAA IDAYVEKLKK NK
//
