ID A0A0D6TAU0_9RHOB Unreviewed; 758 AA.
AC A0A0D6TAU0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KIX17343.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KIX17343.1};
GN ORFNames=SY26_10130 {ECO:0000313|EMBL:KIX17343.1};
OS Paracoccus sp. 228.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1192054 {ECO:0000313|EMBL:KIX17343.1, ECO:0000313|Proteomes:UP000032743};
RN [1] {ECO:0000313|EMBL:KIX17343.1, ECO:0000313|Proteomes:UP000032743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=361 {ECO:0000313|EMBL:KIX17343.1,
RC ECO:0000313|Proteomes:UP000032743};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-2015) 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 -!- 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:KIX17343.1}.
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DR EMBL; JYGY01000003; KIX17343.1; -; Genomic_DNA.
DR RefSeq; WP_046000429.1; NZ_JYGY01000003.1.
DR AlphaFoldDB; A0A0D6TAU0; -.
DR STRING; 1192054.SY26_10130; -.
DR PATRIC; fig|1603292.4.peg.2168; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000032743; 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:KIX17343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032743}.
FT DOMAIN 24..157
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 169..405
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 82..89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 168
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 293
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 758 AA; 81531 MW; 804748D97918C18A CRC64;
MTDKTSRSRI TPEEALAYHL EPRPGKYDIT PSTPMTTQRD LSLAYSPGVA VPVQAIADRP
ETAYDYTTKG NMVAVISNGT AILGMGNLGA LASKPVMEGK AVLFKRFADV NAIDLELDTE
DADEFINAVK LMGPTFGGIN LEDIKAPECF IIEQRLKELM DIPVFHDDQH GTAVICAAGL
LNALELSGKK IEDVRIVLNG AGAAGIACLE LLKSMGARHD NCIMCDTKGV IYQGRTEGMN
QWKSAHAVVT TARTLEEAMK GADVFLGVSA KGAVTQDMVV SMADNPVIFA MANPDPEITP
EDAHAVRPDA IVATGRSDYP NQVNNVLGFP YLFRGALDIH ARAINDEMKI ACAEALAKLA
REDVPDEVAV AYGRKLQFGR DYIIPTPFDP RLIHVIPPAV AKAGMDTGVA RRPIIDMEGY
VQTLKNRMDP TAAILQGIHA RARQAQARMI FAEGDDPRVL RAAVAWQRTG MGQSLVVGRE
AEVKAELEAL GMGDAFREIS VVNAANTRHL DSYHEFLYQR LQRKGVDRED AFKLANRDRH
IFAALMLAHG HGDGLVTGAT RKNAPVLAQI GHVFDVRPQD GAVGITAVLH RGRIVLIGDT
LVHEWPEPED LADIAARGAA VARNLGLEPR VAFLSFSNFG YPVSERAIKM AQAATVLDRR
GADFEYEGEM TVDVALNMDA AARYPFSRLT APANVLVVPA RHSASISVKL MQEMAGATVI
GPILTGVARP IQICSTNSTV SDILNMAAIA AGGVGAQG
//
