ID F9U9S2_9GAMM Unreviewed; 795 AA.
AC F9U9S2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+)) {ECO:0000313|EMBL:EGV18870.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:EGV18870.1};
GN ORFNames=ThimaDRAFT_1674 {ECO:0000313|EMBL:EGV18870.1};
OS Thiocapsa marina 5811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV18870.1, ECO:0000313|Proteomes:UP000005459};
RN [1] {ECO:0000313|EMBL:EGV18870.1, ECO:0000313|Proteomes:UP000005459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5811 {ECO:0000313|EMBL:EGV18870.1,
RC ECO:0000313|Proteomes:UP000005459};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA Bryant D., Woyke T.J.;
RT "The draft genome of Thiocapsa marina 5811.";
RL Submitted (JUN-2011) 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; AFWV01000005; EGV18870.1; -; Genomic_DNA.
DR AlphaFoldDB; F9U9S2; -.
DR STRING; 768671.ThimaDRAFT_1674; -.
DR PATRIC; fig|768671.3.peg.1781; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000005459; 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:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EGV18870.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005459}.
FT DOMAIN 25..158
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 170..407
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 83..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 294
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 795 AA; 84727 MW; 40C5834803255EC7 CRC64;
MTSTLSTAEQ ALREAAREYH RSPSRGKIAV TPSKPLSNQR DLSLAYSPGV AYPCLDIQAD
PALAAEYTAR GNLVGVVTNG TAVLGLGDIG PLAGKPVMEG KGCLFKKFAG IDVFDIELAE
RDPDKLVEII AALEPTLGGI NLEDIKAPEC FYIERELSKR MNIPVFHDDQ HGTAIISSAA
LLNALELVGK AIDTVKLAVS GAGAAALACV DVMVGLGMRR EHVFMVDSKG VIYEGRPGGF
DASKARYAQQ TDARTLADVV EGADVFLGCS APGVLTVEMV KSMADRPIIL ALANPEPEIR
PELAKLARPD CIIATGRSDY PNQVNNVLCF PYIFRGALDC GATKITAEMK LACVRQIADL
AKSETSAEVA TAYAGQDLSF GPDYLIPKPF DTRLILRIAP AVAQAAADSG VATRPIADMQ
AYRDSLTLFV YQTGILMRPV INAAKALPED RKRVAFADGE DERALRAAQI ALDDRLARPI
LIGRPAVIQA HIEKAGLRMR LGEDVENVNP EQDPRFNQYR DHYHRLMGRN GVTPEVAAAA
VRRSNTIIGS LMVALGHADA MICGLAGSYE THLERIHSII GLRPGVSNYA ALNALMTERG
GPLFIADTYV NEDPGAEQLA DIAWMAVQEI QRFGLPAKVA FLSHSSFGSS KRASARKMRL
ARDLFVASHP EIECDGELHG DAALEEDIRS RYLADSTLAG SANLLICPNL DAANILYTVL
KTTTSGGVTV GPILMGAAAT ACILTPAATV RRTLNMTTLA VASAAAARDV PDGSHATLVD
DLPAASRGQP RHALA
//
