ID A0A1Q8YGQ2_9BURK Unreviewed; 775 AA.
AC A0A1Q8YGQ2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:OLP07182.1};
DE EC=1.1.1.39 {ECO:0000313|EMBL:OLP07182.1};
GN Name=maeB {ECO:0000313|EMBL:OLP07182.1};
GN ORFNames=BLL52_1469 {ECO:0000313|EMBL:OLP07182.1};
OS Rhodoferax antarcticus ANT.BR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1111071 {ECO:0000313|EMBL:OLP07182.1, ECO:0000313|Proteomes:UP000185911};
RN [1] {ECO:0000313|EMBL:OLP07182.1, ECO:0000313|Proteomes:UP000185911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANT.BR {ECO:0000313|EMBL:OLP07182.1,
RC ECO:0000313|Proteomes:UP000185911};
RA Baker J., Riester C., Skinner B., Newell A., Swingley W., Madigan M.,
RA Jung D., Asao M., Chen M., Loughlin P., Pan H., Lin S., Li N., Shaw J.,
RA Prado M., Sherman C., Li X., Tang J., Blankenship R., Zhao T., Touchman J.,
RA Sattley M.;
RT "Genome sequence of Rhodoferax antarcticus ANT.BR, a psychrophilic purple
RT nonsulfur bacterium from an Antarctic microbial mat.";
RL Submitted (JAN-2017) 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:OLP07182.1}.
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DR EMBL; MSYM01000009; OLP07182.1; -; Genomic_DNA.
DR RefSeq; WP_075585928.1; NZ_MSYM01000009.1.
DR AlphaFoldDB; A0A1Q8YGQ2; -.
DR STRING; 81479.RA876_01825; -.
DR Proteomes; UP000185911; Unassembled WGS sequence.
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:OLP07182.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185911}.
FT DOMAIN 26..160
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 172..409
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 102
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 84..91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 171
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 296
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 775 AA; 84145 MW; 482301BFB529E704 CRC64;
MTHNSPEEKS AQLRRAALDY HQLPSPGKIA IAATKQLTNQ HDLALAYSPG VAAPCEEIVK
DPNNAHRYTS RGNLVAVITN GTAVLGMGDI GPLAAKPVME GKAVLFKKFA GIDVFDLEIN
EKHDLDKLVD IIASLEPTFG GINLEDIKAP DCFYVERKLR ERMKIPVFHD DQHGTAIVVG
AAILNGLKVV GKDPAKVKLV TSGAGAAALA CLGLLVKLGI ARENIFVTDL AGVVYEGRTE
LMDDDKAFFA QKTSFRTLDE VMKGADVFLG LSAGGVLKGH MVAKMAANPL VFALANPTPE
ILPEEVKAVR SDAIIATGRT DYPNQVNNVL CFPYIFRGAL DAGASTITLE MEIAAVHAIA
ELARAEQSEV VVAAYAGERL TFGREYLIPK PFDPRLMVVI APAVAKAAAD SGVATRPIGD
FTAYREQLQS FVYASGTMMK QIFTAAKKAA HKRVAYCEGE EERVLRACQI VVDEGLARPT
LIGRPAVIAQ RIKKFGLRLE EELDYDVVNV EKDDRYRDFW QSYHQMTERK GVSVHAAKID
MRRRLTLIGS MLLHKGYVDG IVCGTWGTTQ LHLHYIDQVI GKRSRSSLNS TQDVQIYACM
NGLMLPDRQL FLVDTHVNYD PTAQELATIT VMAAEEMKHF GMHPRAALLS HSNFGSSNQP
SAVKMRQTLE LLRVQAPWLE VEGEMHGDLA LDSAARHAMM PHSTLAGDAN LLVLPNIDAA
NIAYNLLKVT AGGNIAVGPV LLGAAKPVHI LTASTTVRRI VNMTALTVAD ANANR
//
