ID A0A345GYW2_9FLAO Unreviewed; 767 AA.
AC A0A345GYW2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:AXG69500.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:AXG69500.1};
GN Name=maeB {ECO:0000313|EMBL:AXG69500.1};
GN ORFNames=KORDIASMS9_01723 {ECO:0000313|EMBL:AXG69500.1};
OS Kordia sp. SMS9.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=2282170 {ECO:0000313|EMBL:AXG69500.1, ECO:0000313|Proteomes:UP000253780};
RN [1] {ECO:0000313|EMBL:AXG69500.1, ECO:0000313|Proteomes:UP000253780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS9 {ECO:0000313|EMBL:AXG69500.1,
RC ECO:0000313|Proteomes:UP000253780};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Clarke A.K.,
RA Godhe A.;
RT "Genome Sequence of Kordia sp. Strain SMS9 Isolated from a Culture of the
RT Diatom Skeletonema marinoi.";
RL Submitted (JUL-2018) 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; CP031153; AXG69500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345GYW2; -.
DR KEGG; kos:KORDIASMS9_01723; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000253780; 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:AXG69500.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253780}.
FT DOMAIN 22..155
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 167..403
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 80..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 290
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 767 AA; 85489 MW; 6AB151C927DF3A84 CRC64;
MSKSNKERKR REALIYHAKP RPGKIKVVPT KRYSTQRDLS LAYSPGVAEP CLEIKKDKKN
VYKYTTKGNL VAVISNGTAV LGLGDIGPEA SKPVMEGKGL LFKIFADIDV FDIEVDTKDV
DQFIETVKNI APTFGGINLE DIKAPEAFEI ERRLIEELDI PVMHDDQHGT AIISSAALIN
ALELAEKNIE EVRIVVSGAG SAAISCMNLY VALGAKLENI AMFDVDGLLH KGRTDLSPMQ
AHFRTDKHYD SLADALKGAD VFLGLSVGNI VSQDMLRSMA HDPIVFAMAN PTPEISYEEA
IVSRKDIIMA TGRSDHPNQV NNVLGFPFIF RGALDVRATK INEAMKMAAV KALAELAKEP
VPEQVNIAYA ETKLTFGKEY IIPKPFDPRL IAKIPPAIAK AAMDSGVATE PIEDWARYED
ELLHRLDADN KIIRLLHKRA RSNKKRIVFA EADHLDVLKA AQYVYDERIA IPILLGNEKR
IHELRDELEF DGDVEIIDPK SDEQRARRHK FAEIYWETRK RKGVTKIDAK KMMRERNYFA
AMLVNDGYAD GLISGYSRSY PTVVKPMLEL IGTAKGVRKA ATTNLMITER GPIFLSDTSI
NIDPSARDLA KIVQMTAMTV KMFGLEPNIA MLSYSNFGSS EHEDAKKVGE AVDYLHRYYP
NINVDGAVQS DFALNREMLS EKFPFSKLAG KEVNTLVFPN LDSANITYKL MKELNKADSI
GPIMLGMKKP VHILQLGASV DEIINMAAVA AVDAQEKEKW QQRKEEE
//
