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Database: UniProt
Entry: A0A2I0R6D9_9FLAO
LinkDB: A0A2I0R6D9_9FLAO
Original site: A0A2I0R6D9_9FLAO 
ID   A0A2I0R6D9_9FLAO        Unreviewed;       755 AA.
AC   A0A2I0R6D9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:PKR82153.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:PKR82153.1};
GN   ORFNames=CW751_02110 {ECO:0000313|EMBL:PKR82153.1};
OS   Brumimicrobium salinarum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Crocinitomicaceae; Brumimicrobium.
OX   NCBI_TaxID=2058658 {ECO:0000313|EMBL:PKR82153.1, ECO:0000313|Proteomes:UP000236654};
RN   [1] {ECO:0000313|EMBL:PKR82153.1, ECO:0000313|Proteomes:UP000236654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHR20 {ECO:0000313|EMBL:PKR82153.1,
RC   ECO:0000313|Proteomes:UP000236654};
RA   Do Z.-J., Luo H.-R.;
RT   "The draft genome sequence of Brumimicrobium saltpan LHR20.";
RL   Submitted (DEC-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}.
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:PKR82153.1}.
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DR   EMBL; PJNI01000001; PKR82153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0R6D9; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000236654; Unassembled WGS sequence.
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:PKR82153.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236654}.
FT   DOMAIN          18..151
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          163..400
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         76..83
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         162
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   755 AA;  82993 MW;  8399CE61D07D8C64 CRC64;
     MAKIKKQDAL DYHSQGKPGK IEVIPTKPYS SQRDLSLAYS PGVAEPCLKI AENPDDVYKY
     TAKSNLVAVI SNGTAVLGLG DIGPAASKPV MEGKGLLFKI FADIDVFDIE VDANDPETFI
     QTVKAIAPTF GGINLEDIKA PEAFEIEDRL KEELDIPVMH DDQHGTAIIS SAGLINALEL
     ADKKIEEVKI VVSGAGASAM SCAKLYNSLG AKMENIFMFD SKGLLSKDRE NLSGNKAFFA
     EHHENTSDLA TELKGADVLI GLSRGGVVSK QMVKSMADNP IVFALANPEP EIAYDDAMSV
     RKDVIMATGR SDHPNQVNNV LGFPFIFRGA LDVRAKSINE EMKLAAVYAI ANLAKETVPD
     EVSEAYGERS ITFGRDQFIP KPLDPRLIYY VAPAVAKAAM DSGVARTPIE DWDAYDAELK
     KRLGIDNKLV RTITDKAERN PKRVVFAEAD NYKILKAAQT AMEEGVATPI LLGRKEKVLH
     MIEEYNMDFP DVEVVDPKDI GEKDRLERYA EAFFELRQRK GFTAYEASKI MRERNYFGAM
     MVQSGDADAM ISGATRKYSD VLRPALQVIG TQKDVDRVAG MYILITKRGP IFMADTTVNF
     DPTAEEIADM THHIAKTIRK FKVNPNIALL SYSNFGSAEG KDAKKMAKAV EIIHDKYPTL
     RVDGEVQANF ALNNELMNEK FAFSELTNKK VNTFIFPNLS AGNIAYKLLQ EMTEAEAIGP
     VLVGLRKSVH VLQLGASVRE IVNMVKVAVV DAQNK
//
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