ID F4QK35_9CAUL Unreviewed; 760 AA.
AC F4QK35;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:EGF92062.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:EGF92062.1};
GN ORFNames=ABI_04940 {ECO:0000313|EMBL:EGF92062.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF92062.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; GL883077; EGF92062.1; -; Genomic_DNA.
DR RefSeq; WP_006271232.1; NZ_GL883077.1.
DR AlphaFoldDB; F4QK35; -.
DR STRING; 715226.ABI_04940; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000006512; 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; IPR015884; Malic_enzyme_CS.
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.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW 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:EGF92062.1}.
FT DOMAIN 22..155
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 167..404
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 80..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 291
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 760 AA; 82393 MW; 4B31425630A4DD42 CRC64;
MPSEKQTFSD DEALYLHQYP QPGKIALLPT KPMATQRDLA LAYSPGVAVP VRRIAENPET
AYDYTAKGNM VAVISNGTAI LGLGNLGALA SKPVMEGKAV LFKRFGDIDS FDIEVTTQDP
DEFITVVKNI TASFGGINLE DIKSPECFII EAALQDLADI PVFHDDQHGT AIIAAAGLIN
ALEITGKRIE DVKVVLCGAG AAGLSSLSLI KALGVRHDNT TVVDIHGVVF EGRKVDMDQW
KSAHATRTNK RTLAEAMVGA DVFLGLSARG VLTSDMVATM AANPIIFAMA NPDPEITPED
VAKVRSDAIV ATGRSDYPNQ VNNVLGFPYI FRGALDVRAR RVNHEMKLAA AKALAMLARE
DVPDEVAAAY QGRHLKFGKD YIIPSPFDPR LLWYVPPFVA QAAMDTGVAR KPITDMDAYR
KSLEQRLDPS AGLLQNITST VRSRPAKRIV FAEGEDISVI RAAHAFKQSG LGIPLLCGRE
NLIRDNMRVA GLNPDEEDIE IINARKSHRR DAYAQLLYAR LQRKGYLKRD VERLINLDRN
SFAAAMLMSG HADGMVTGVT RAFDQAFEEV MRVVDPAPGG RIMGMSIVLA RGKTLFIADT
TVSELPSPEE LGDIAIEAAT AVRNMGHTPR VAFMSYSNFG NPAGERSERV SQAVRLLEQR
GVDFEFEGEM SPEIALDSAR WVNYPFQRLT APANVLIMPA IHSASISTNL IEAIGGATVV
GPLLLGLSKP VQICQLSDSV SKILTMATFA AYDIRASVKV
//
