ID A0A0P0AAE3_9RHOB Unreviewed; 753 AA.
AC A0A0P0AAE3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:SFL04609.1};
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:ALI55732.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ALI55732.1};
GN ORFNames=IMCC12053_1785 {ECO:0000313|EMBL:ALI55732.1},
GN SAMN05444421_11432 {ECO:0000313|EMBL:SFL04609.1};
OS Celeribacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI55732.1, ECO:0000313|Proteomes:UP000064920};
RN [1] {ECO:0000313|EMBL:ALI55732.1, ECO:0000313|Proteomes:UP000064920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI55732.1,
RC ECO:0000313|Proteomes:UP000064920};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SFL04609.1, ECO:0000313|Proteomes:UP000181863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100036 {ECO:0000313|EMBL:SFL04609.1,
RC ECO:0000313|Proteomes:UP000181863};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012023; ALI55732.1; -; Genomic_DNA.
DR EMBL; FOSM01000014; SFL04609.1; -; Genomic_DNA.
DR RefSeq; WP_062218149.1; NZ_FOSM01000014.1.
DR AlphaFoldDB; A0A0P0AAE3; -.
DR STRING; 1397108.IMCC12053_1785; -.
DR KEGG; cmar:IMCC12053_1785; -.
DR PATRIC; fig|1397108.4.peg.1822; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000064920; Chromosome.
DR Proteomes; UP000181863; 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:ALI55732.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000064920}.
FT DOMAIN 20..153
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 165..401
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 78..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 164
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 289
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 753 AA; 80452 MW; A9460BAC2082DD39 CRC64;
MSKIKQTREE ALAFHMDPRP GKFDIAPSVP MSTQRDLSLA YSPGVAVPCE AIAANPETAY
DYTNKGNLVA VISNGTAVLG LGNLGALASK PVMEGKAVLF KRFADVNSID IELDTEDPDQ
IIQAVKLMGP TFGGINLEDI KAPECFIIEQ KLKEEMDIPV FHDDQHGTAV ICAAGLINAL
HISGKCIEDC KIVLNGAGAA GIACLELIKS MGAKHDNCIM CDTKGVIYQG RTEGMNQWKS
AHAAKTDART LGEAMVGADV FLGVSAKGAV TSDMVAAMAP NAVIFAMANP DPEITPEDAH
AVREDVIVAT GRSDYPNQVN NVLGFPYLFR GALDIHARAI NDEMKIACAE ALAALAREDV
PDEVALAYGR SLTFGRDYII PTPFDPRLIY TIPPAVAKAG MDTGVARRPI VDMDGYAHGL
KARMDPTAQI LQGLYARARQ AQATMLFAEG DDLRVLRAAV AYQRGGYGKA LIVGRDEDVN
AKLNEAGLSD AAGELEIVNA ANTPHLDSYK AFLYDRLQRS GHDQKDIHRL AARDRHAFSA
LMLAHGHADG LVTGATRKSA HVLDRINSVF DATAEDGAIG VSALIHNGRI VFIADTLVHE
WPDEHDLADI AEAAAKVARS MGIEPRVAFA SFSTFGYPVS ERASKMHLAP KVLDSRKVDF
EYDGEMTVEV ALNTDAMAAY PFCRLTGPAN ILVVPARHSA SISVKLMQEM AGATVIGPIL
TGVDKPIQVC STVSTVNDIL NMAILAACKV GQS
//
