ID Q6FA39_ACIAD Unreviewed; 756 AA.
AC Q6FA39;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=Putative bifunctional protein (MaeB) {ECO:0000313|EMBL:CAG69074.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:CAG69074.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:CAG69074.1};
GN OrderedLocusNames=ACIAD2287 {ECO:0000313|EMBL:CAG69074.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG69074.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG69074.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG69074.1; -; Genomic_DNA.
DR RefSeq; WP_004927971.1; NC_005966.1.
DR AlphaFoldDB; Q6FA39; -.
DR STRING; 202950.GCA_001485005_00114; -.
DR GeneID; 45234610; -.
DR KEGG; aci:ACIAD2287; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_6; -.
DR OrthoDB; 9805787at2; -.
DR BioCyc; ASP62977:ACIAD_RS10460-MONOMER; -.
DR Proteomes; UP000000430; Chromosome.
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:0008959; F:phosphate acetyltransferase 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; 2.
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 Acyltransferase {ECO:0000313|EMBL:CAG69074.1};
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:CAG69074.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430};
KW Transferase {ECO:0000313|EMBL:CAG69074.1}.
FT DOMAIN 19..152
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 164..397
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 77..84
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 163
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 756 AA; 82440 MW; 8EF9D11238AA6A0B CRC64;
MDDQSLKQAA LYYHENPTPG KISVTPSKQL VNQHDLALAY SPGVAAPCLE IERDPSTAAK
YTARGNLVAV VTNGTAVLGL GNIGPLASKP VMEGKGVLFK KFAGVDVFDI EIAENDPDKI
VDIVAALEPT FGGINLEDIK APECFYIEKK LRERMNIPVF HDDQHGTSII VGSALLNALQ
LVNKKIEDIK IVASGAGAAA LSCLDLLCAL GARKENIIVA DSRGLLTTSR DGLDESKKRY
VQDITATQLH EVITGADMFL GLSAAGILTK EMVKGMAENP IIFALANPDP EILPEHAHEV
RPDVIMATGR SDYPNQVNNA LCFPYIFRGA LDVGATTINE DMKIACVHAI ARMAHVEADA
ATYGEKSASF GRDYLIPRPL DQRLILEIAP AVAQAAMDSG VATRPIEDFS AYRQKLSEFV
YNSAFIMKPI FSQAKADPKR IAYAEGEDYR VLRTAQIVVD DGIAFPVLVG RTAVIEANIK
KLGLRLENGV NIEIVDQENN PLYEEFWKDY YQIMQRKGVT VEYAQREARR RSTLIAAMLV
KFGKADGMLC GTYSSYDIHL DFVSKVIGLK EGMNNFFTLN ALMLEDRNLF IADTYVNTNP
TAEQLADMTI LAAEEVRRFG ITPRVALLSH SSFGSNQEDP SAQKMREVYR LLNERAPELE
VEGEMHGDAA LDESIRHSAF PGSNFKGSAN LLIMPNLDAA NISFNLLKAT SGNNVTIGPI
LLGAAKPVHI LTPTATTRRV LNMTALTVAE IQQSEG
//
