ID A0A1U7PUM2_9FLAO Unreviewed; 760 AA.
AC A0A1U7PUM2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:SIT97256.1};
GN ORFNames=SAMN05660493_01969 {ECO:0000313|EMBL:SIT97256.1};
OS Epilithonimonas bovis DSM 19482.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=1121284 {ECO:0000313|EMBL:SIT97256.1, ECO:0000313|Proteomes:UP000187261};
RN [1] {ECO:0000313|Proteomes:UP000187261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19482 {ECO:0000313|Proteomes:UP000187261};
RA Varghese N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FTPU01000019; SIT97256.1; -; Genomic_DNA.
DR RefSeq; WP_076783432.1; NZ_FTPU01000019.1.
DR AlphaFoldDB; A0A1U7PUM2; -.
DR STRING; 1121284.SAMN05660493_01969; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000187261; 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; 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}.
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 REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 292
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 760 AA; 83715 MW; DE9C7167B9A945D1 CRC64;
MSKNSRDQNA FDKAALDYHS QEPKGKIEVI PSKPHSSQRD LSLAYSPGVA VPCMAIHDNP
QSVYDYTSKG NLVAVISNGT AVLGLGDIGP EASKPVMEGK GLLFKIFAGI NVFDIEINEK
DPDKFIETVK AIAPTFGGIN LEDIKAPEAF YIEQRLKEEL DIPLMHDDQH GTAIISAAAL
INALEIAGKK IAEVKMVING AGAAAIACAK LYISLGLNPD NILMCDSKGV INHKRENLTP
EKLDFVSQTN IATLEEALKG ADVFVGLSKG NVMSPEMLLS MAEKPIVFAL ANPDPEISYD
LAVATRPDVM MATGRSDYPN QVNNVLGFPY IFRGALDVQA RGINEAMKLA AVYALAEIAK
EPVPEMVKLA YNVRDISFGK DYFIPKPFDN RLITKVSMAV AKAAMESGIA GKSIENFEEY
ENQLLDRMGR DEKLVRMMQN RAKANPKRVT LGNGEEYNIL KAAQILQEEG IAYPSLLGNK
KLIREKMEEY GITLDIPIID PNDDEQKESR KKFRKTLWDK RNRKGINEYK AKRYVRQRDY
FGPLMLEHGD TDALIVGFSK SYASVLKPVL EIIDKKPGVN KVAAMMMILT EKKPLFFADT
SINKNPSAED LVDIARMAEI TVKSFAIDPR IAMLGFENFS AKADTSKKVA AAVKMLHEKF
PKMVVDGEIQ PDFALNADHL ADYPFSKLGS NPANVLVFPN LESANLSYKI IRGMKAAQTI
GPILMGLNQP VHVLQMRSSV DEIVNLATIA VLDAQMKDKK
//
