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Database: UniProt
Entry: A0A316EEH0_9BACT
LinkDB: A0A316EEH0_9BACT
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ID   A0A316EEH0_9BACT        Unreviewed;       757 AA.
AC   A0A316EEH0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:PWK28470.1};
GN   ORFNames=LV89_00674 {ECO:0000313|EMBL:PWK28470.1};
OS   Arcicella aurantiaca.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Arcicella.
OX   NCBI_TaxID=591202 {ECO:0000313|EMBL:PWK28470.1, ECO:0000313|Proteomes:UP000245489};
RN   [1] {ECO:0000313|EMBL:PWK28470.1, ECO:0000313|Proteomes:UP000245489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22214 {ECO:0000313|EMBL:PWK28470.1,
RC   ECO:0000313|Proteomes:UP000245489};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAY-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWK28470.1}.
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DR   EMBL; QGGO01000003; PWK28470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316EEH0; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000245489; 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:UP000245489}.
FT   DOMAIN          20..153
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          165..402
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        96
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         78..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         138
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         139
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         164
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         289
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ   SEQUENCE   757 AA;  83415 MW;  94808F027D9CA57A CRC64;
     MSQKPIRKQD ALDYHSKGRP GKIAVISTKE TETQRDLSLA YSPGVAEPCL EIAANKENVY
     KYTAKGNLVA VISNGTAVLG LGNIGPEASK PVMEGKGVLF KIFADIDVFD IELNTEDPEE
     VIRTVKILEP TFGGVNLEDI KSPECFEIEE RLRKDLNIPI MHDDQHGTAI ISGAALLNAL
     EIVDKKIEEC RFVVSGAGAA ALSCMKLYLG LGAKVENLLM FDKDGLVSKS RTDLNKYVQP
     FASDRTDIHS LADAMVGADV FLGLSVGNIV SQDMIKTMAK DAVVFAMANP TPEIAYEDAV
     AAREDIIMAT GRSDYPNQVN NVLGFPYIFR GALDVRATEI DENMKMAAAK ALAELAKKPV
     PDIVNLAYNE KNLTFGRNYI IPKPVDPRLI TTVAPAVARA AMESGLAQSP IADWDAYELE
     LSKRLGLDNQ LMKYIVNRAK RSPKRVVFAD AENLKVLKAV QQSKDERICI PILLGDVQKI
     KGIIETNNLD LCDVEIIDTR SPETAERLKH YGDLFFEKRK RKGYNHYEAH KQMQVRSYFA
     AMMVETGDAD CVISGLTRNY PDAIRPALQI IGREDGVKKV SGMYILLTKK GPIFFSDTTI
     NFDPTVEDIV EITELTAKAV EQFNLKPRIA LLTYSNFGTA NGDDAVKMRE ATAILQKKHP
     EMIVEGEMQA HLAFDNELIK ENYPFSKLAE EGANTLIFPN LSAANIAYNL LKETSDIEYI
     GPILLGLRKP VHVLQLGSSV REIVNMVAIA VVEAQGK
//
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