ID K9VHV6_9CYAN Unreviewed; 463 AA.
AC K9VHV6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+)) {ECO:0000313|EMBL:AFZ07688.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:AFZ07688.1};
GN ORFNames=Osc7112_3306 {ECO:0000313|EMBL:AFZ07688.1};
OS Oscillatoria nigro-viridis PCC 7112.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ07688.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ07688.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ07688.1,
RC ECO:0000313|Proteomes:UP000010478};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003614; AFZ07688.1; -; Genomic_DNA.
DR RefSeq; WP_015176956.1; NC_019729.1.
DR AlphaFoldDB; K9VHV6; -.
DR STRING; 179408.Osc7112_3306; -.
DR KEGG; oni:Osc7112_3306; -.
DR PATRIC; fig|179408.3.peg.4063; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_3; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000010478; Chromosome.
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 CDD; cd04887; ACT_MalLac-Enz; 1.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.30.70.260; -; 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; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000313|EMBL:AFZ07688.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010478}.
FT DOMAIN 13..89
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 213
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 238
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 463 AA; 49038 MW; 12B5D950B430B8AD CRC64;
MVKLTPNPSF SLTIRVALPN QPGMLARVTS AIASVGGNFG QIDLIEQTRA TTVRDITVDA
SSIEHNEEIV QAVKGLPDIK VIDVYDRTFN LHRGGKISVV SKISLKRQSD LAMAYTPGVG
RICTAIANDP QQVYNLTIKQ NTVAIVTDGS AVLGLGNLGA AAALPVMEGK AMLFKEFAGI
DAFPICLNTQ DTEEIIRTVQ NIAPVFGGVN LEDISSPRCF EIEARLRETL DIPIFHDDQH
GTAIVSLAAL INALKIVKKT IAEVCIVING AGAAGVAIAR LLRKAGAQNI IMCDSKGVLS
QDRTDMNPEK LEFAVPSSGT LEDAIAGADV FLGVSAPGVL TRSMVRSMAE NPIVFAMANP
IPEIQPELIM EDAAIVATGR SDYPNQINNV LAFPGIFRGA LDCKAATITP SMYLEAAYAI
ASLVSPSGLD KEHIIPSVFD ERVAIAVAGA VQLAARSEGI ARD
//
