ID A0A1H7YUQ5_9RHOB Unreviewed; 760 AA.
AC A0A1H7YUQ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:SEM49108.1};
GN ORFNames=SAMN04488003_101296 {ECO:0000313|EMBL:SEM49108.1};
OS Loktanella fryxellensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=245187 {ECO:0000313|EMBL:SEM49108.1, ECO:0000313|Proteomes:UP000199585};
RN [1] {ECO:0000313|EMBL:SEM49108.1, ECO:0000313|Proteomes:UP000199585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16213 {ECO:0000313|EMBL:SEM49108.1,
RC ECO:0000313|Proteomes:UP000199585};
RA de Groot N.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 -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; FOCI01000001; SEM49108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7YUQ5; -.
DR STRING; 245187.SAMN04488003_101296; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000199585; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000199585}.
FT DOMAIN 23..156
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 168..405
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 81..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 167
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; 81454 MW; 15D46E13369CA6D8 CRC64;
MSDDTPSDSL RKAALEYHQF PRPGKLEIRA TKPLANGRDL ARAYSPGVAE ACLEIKRDPG
TARDYTTRGN LVGVVTNGTA VLGLGNIGAL ASKPVMEGKA VLFKKFANID CFDIELNEPD
PVKLAEIVCA LEPTFGAINL EDIKAPDCFV VEEICRQRMN IPVFHDDQHG TAIVVGAGIT
NALKIARKNF ADVKVVSTGG GAAGIACLNM LLKLGVRREN VFLCDLAGLV YNGRTADMTD
QKAAYAQGDA PRTLDDVIAG ADVFLGLSGP GVLTPAMVGR MADVPIIFAL ANPSPEIDPA
AARAVNPRAI IATGRSDFPN QVNNVLCFPF IFRGALDAGA TTINDEMKIA CIEGIAAMAR
ATTSAEAAAA YQGEQLTFGP EYLIPKPFDP RLMGVVASAV ARAAGETGVA TRPIADMDAY
KRQLDASVFK SALIMRPVFA AARAVSRRIV FAEGEDERVL RTAQAIMEDT TEVPILIGRP
DVIVARCERA GLDIRPDTHF EVVNPESDSR YRDYWGTYHE IMARKGVTPD LARAVMRTNT
TAIGAVMVQR NEADSLICGT FGQYLWHLNY IQQILGTAAM QPVAALSLMI LESDTLFIAD
TQVHEEPTPQ QIADTVIGAA RHIRRFGVEP RIALCSHSQF GNLDSNSGRR MRAAMDILHG
TPRDFAFEGE MHIDSALDVD LRARIFPGAH LDGPANCLVF ANADAASGVR NILKMKGNAL
EVGPILMGMG NRAHIVTPSI TARGLLNMSA IAGTPVAHYG
//
