ID A0A1T5L785_9BACT Unreviewed; 759 AA.
AC A0A1T5L785;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:SKC71790.1};
GN ORFNames=SAMN05660236_2666 {ECO:0000313|EMBL:SKC71790.1};
OS Ohtaekwangia koreensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Ohtaekwangia.
OX NCBI_TaxID=688867 {ECO:0000313|EMBL:SKC71790.1, ECO:0000313|Proteomes:UP000190961};
RN [1] {ECO:0000313|EMBL:SKC71790.1, ECO:0000313|Proteomes:UP000190961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25262 {ECO:0000313|EMBL:SKC71790.1,
RC ECO:0000313|Proteomes:UP000190961};
RA Peterson S.W.;
RL Submitted (FEB-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; FUZU01000002; SKC71790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5L785; -.
DR STRING; 688867.SAMN05660236_2666; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000190961; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000190961}.
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 759 AA; 83429 MW; A3E9C8CCE0952EDB CRC64;
MSIKIRKEDA LNYHMQGQPG KIEVVPTKVL SSQRDLALAY SPGVAEPCKE IAANKEDVYK
YTSKGNLVAV ISNGTAVLGL GDIGPEASKP VMEGKGVLFK KFAGIDVFDI EIDEKDPDEL
IKIIKSLEPT FGGVNLEDIK APECFKIETE LREKMNIPIM HDDQHGTAII SCAALLNALE
IVEKKMEDIK IVVNGAGAAA VSCTKLYIAL GARKENIIMC DSKGVLNTSR TNLDDIKKQF
VSDVKINTLQ EAMKGADVFI GLSVADAITP EDLNNMAKDP IVFALSNPNP EIDYNLARKT
REDAILATGR SDHPNQVNNV LGFPYIFRGA LDVRATEINE AMKLAAVHAL ADLAKEPVPD
MVVKAYGTDK IQFGREYLIP KPLDPRLITT VSPAVAKAAM DSGIAKYPIT DWAAYHHQLQ
QRIGIDQKLM SRVIDRAKKN PKRVVFAEAN HHKILKAAQI LKDEGIAKPI LLGNREEIHK
LIEEYNLDLH DCPIYYPRED DDMVNRYAEV LYKKRQRKGL TYLDSVRMMR ERNYFGAMMV
EFGDADALVS GLTKDYPKTI LPSLQIIGTA EGVNRVAGMY IIVNKKGTFF FADTTVNVDP
NAQELAGIIE LTARGVKFFD MDPRIAVLSY SNFGSSQGEV PEKSREAVRI AKAKNPSLVV
EGDIQANVAL NTQLQQETFP FSALAQEGAN TLIFPNLASG NIAYKLLMEL GGAEAIGPIL
LGMKKPVHVL QLGSSIREIV NMAAIAVVDA QLHEQNDHL
//
