ID K2J4F2_9RHOB Unreviewed; 764 AA.
AC K2J4F2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:EKE69752.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:EKE69752.1};
GN ORFNames=B30_15466 {ECO:0000313|EMBL:EKE69752.1};
OS Celeribacter baekdonensis B30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE69752.1, ECO:0000313|Proteomes:UP000006762};
RN [1] {ECO:0000313|EMBL:EKE69752.1, ECO:0000313|Proteomes:UP000006762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B30 {ECO:0000313|EMBL:EKE69752.1,
RC ECO:0000313|Proteomes:UP000006762};
RA Wang W.;
RT "Celeribacter baekdonensis B30 Genome Sequencing.";
RL Submitted (SEP-2012) 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:EKE69752.1}.
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DR EMBL; AMRK01000009; EKE69752.1; -; Genomic_DNA.
DR RefSeq; WP_009573074.1; NZ_AMRK01000009.1.
DR AlphaFoldDB; K2J4F2; -.
DR STRING; 1208323.B30_15466; -.
DR PATRIC; fig|1208323.3.peg.3200; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000006762; 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; IPR032683; Malate_DH.
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; PF12434; Malate_DH; 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:EKE69752.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006762}.
FT DOMAIN 27..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 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 85..92
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 764 AA; 82789 MW; 0C565B84C8FFC60F CRC64;
MTSDTRTDSR NNSLRQAALD YHEFPKPGKL EIRATKPMAN GRDLARAYSP GVAEACLEIK
ADPSTSSRYT SRGNLVAVVT NGTAVLGLGN IGPAAAKPVM EGKAVLFKKF ANIDCFDIEL
DESDPVKLAE IVCALEPTFG AINLEDIKAP DCFIVEQLCR EKMNIPVFHD DQHGTAIVVG
AAATNALRVT NKKFEDIKVV STGGGAAGIA CLNMLLKLGL KRENVWLCDI AGLVYEGRTE
EMTPQKAAFA QKTDLRTLDD VIEGADLFLG LSGPGVLKPE MVAKMARQPI VFALANPTPE
IHPDEVKKVA PDAIIATGRS DYPNQVNNVL CFPFIFRGAL DVAATEINDA MQIACIEGIA
ALARATTSAE AAAAYQDERM EFGPEYLIPK PFDPRLMGVV ASAVAKAAME SGVATKPVPD
MKAYKDALDH SVFKSALIMR PVFAAASQAE RRIAFAEGED DRVLRAAQAM IEETTDKPIL
IGRPEVIAVR AERAGLKIRP GVDFEIVNPE NDSRYKQYWQ AYHKLMERKG VTPDLAKAIM
RTNTTAIGAI MVHQDHADSM ICGTFGQYLW HLNYVTQILG TKEHQPVGAL SLMILEDGPL
FIADTHVHTE PTPEQIAKTV IATARHVRRF GIEPNIALCS HSEFGNLQCT TGRHMREALE
ILDSEPRDFI YEGEMHIDSA LTPDLRARNF PHSRLEGPAN ALIFAIADAA SGVRNILKTK
GGGLEVGPIL MGMANRAHIV TPSITPRGLL NMSAMAGTPV AHYG
//
