ID A0A2K8X676_9FLAO Unreviewed; 762 AA.
AC A0A2K8X676;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:AUC78427.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:AUC78427.1};
GN ORFNames=CW736_02990 {ECO:0000313|EMBL:AUC78427.1};
OS Nonlabens sp. MB-3u-79.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=2058134 {ECO:0000313|EMBL:AUC78427.1, ECO:0000313|Proteomes:UP000232401};
RN [1] {ECO:0000313|EMBL:AUC78427.1, ECO:0000313|Proteomes:UP000232401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB-3u-79 {ECO:0000313|EMBL:AUC78427.1,
RC ECO:0000313|Proteomes:UP000232401};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-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}.
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DR EMBL; CP025116; AUC78427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8X676; -.
DR KEGG; nob:CW736_02990; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000232401; Chromosome.
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; 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:0000313|EMBL:AUC78427.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000232401}.
FT DOMAIN 19..152
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 164..400
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 762 AA; 83649 MW; C24F41903F4D7D97 CRC64;
MSEESKRREA LIYHAKPTPG KIKVVPTKKH SSQRDLALAY SPGVAAPCLE IAKDKSNVYK
YTAKGNLVAV ISNGTAVLGL GDIGPEASKP VMEGKGLLFK IFADLDCFDI EVDTKDVEEF
IKTVKNIAPT FGGINLEDIK APEAFEIERR LKEELDIPVM HDDQHGTAII SSAALLNALE
IAEKKIEDVK ILISGAGSAA ISCTSLYVKL GARKENIMMF DIDGLITKDR TDLGPEQMQF
ATDQPKVNLR EAFKGTDVFL GLSAGNIVDG DMLKSMNDSP IVFAMANPTP EIDYHTAMAS
REDIIMATGR SDHPNQVNNV LGFPFIFRGA MDVRATKINE EMKLAATYAI AQLAKEPVPE
QVNIAYGELK IAFGRDYIIP KPFDPRLIST IPPAVARAAM ESGVAQEPIT DWDKYTEQLL
SRMGSDNKLV RLLLNRARTN PKRIVFAEAD NIDVLKAAQI VLEEGIGIPI LLGRRDIIEA
LMEDLGFDQP CMIIDPKSDE EKARRDRYAD EFWKLRHRKG TTEFDAGKTL RQRNYFAAMM
VKLGDADALI TGVAQSYPIS VRPMMEIIGK APGVDKIATT NLMITSRGPL FVSDTSININ
PDALELAKIA QMTGRTAAMF GISPVIAMTS YANFGSSKHP NATKVTEAVK YLHKYYPDLV
VDGELQTDFA LNPELLQSKF PFSKLAGKKV NTLIFPNLES ANSSYKMLKE LNGIDSIGPI
MMGMQKPVHI LQLGASVDEI VNMAAVAVID AQQKEKHASK KQ
//
