ID   MCR_METS5               Reviewed;         357 AA.
AC   A4YEN2;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Malonyl CoA reductase (NADP);
DE            EC=1.2.1.75;
DE   AltName: Full=NADP-dependent malonyl CoA reductase;
GN   OrderedLocusNames=Msed_0709;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-20, FUNCTION AS A MALONYL COA REDUCTASE,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=17041055; DOI=10.1128/jb.00987-06;
RA   Alber B., Olinger M., Rieder A., Kockelkorn D., Jobst B., Hugler M.,
RA   Fuchs G.;
RT   "Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for
RT   autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus
RT   spp.";
RL   J. Bacteriol. 188:8551-8559(2006).
CC   -!- FUNCTION: Catalyzes the reduction of malonyl-CoA to malonate
CC       semialdehyde, a key step in the 3-hydroxypropanoate and the 3-
CC       hydroxypropanoate/4-hydroxybutyrate cycles.
CC       {ECO:0000269|PubMed:17041055}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxopropanoate + CoA + NADP(+) = H(+) + malonyl-CoA + NADPH;
CC         Xref=Rhea:RHEA:26446, ChEBI:CHEBI:15378, ChEBI:CHEBI:33190,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.2.1.75;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.1 mM for malonyl-CoA (with 0.5 mM NADP)
CC         {ECO:0000269|PubMed:17041055};
CC       pH dependence:
CC         Optimum pH is 7.8, with half-maximal activities at pH 6.5 and 8.5.
CC         {ECO:0000269|PubMed:17041055};
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius.
CC         {ECO:0000269|PubMed:17041055};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17041055}.
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000682; ABP94884.1; -; Genomic_DNA.
DR   RefSeq; WP_012020671.1; NC_009440.1.
DR   AlphaFoldDB; A4YEN2; -.
DR   SMR; A4YEN2; -.
DR   STRING; 399549.Msed_0709; -.
DR   EnsemblBacteria; ABP94884; ABP94884; Msed_0709.
DR   GeneID; 5103747; -.
DR   GeneID; 59455837; -.
DR   KEGG; mse:Msed_0709; -.
DR   eggNOG; arCOG00494; Archaea.
DR   HOGENOM; CLU_049966_1_0_2; -.
DR   OMA; CEEEMKM; -.
DR   BioCyc; MetaCyc:MON-13726; -.
DR   Proteomes; UP000000242; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00978; asd_EA; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Malonyl CoA reductase (NADP)"
FT                   /id="PRO_0000418854"
FT   ACT_SITE        150
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        245
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..16
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..181
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         332..333
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  39255 MW;  3F04E3ADCD94E3F4 CRC64;
     MRRTLKAAIL GATGLVGIEY VRMLADHPYI KPTYLAGKGS VGKPYGEIVR WQTVGNVPKE
     VANQEVKPTD PKLMDDVDII FSPLPQGAAG PVEEQFAKLG FNVISNSPDH RFDMDVPMII
     PEVNPHTVTL IDEQRKRRDW KGFIVTTPLC TAQGAAIPLT PIYQNFKMSG VMITTMQSLS
     GAGYPGIASL DIVDNALPLG DGYDAKTVKE ITRILSEVKR NVQEPGVNEI TLDATTHRIA
     TIHGHYEVAY VTFKEDTDVR KVMESMESFK GEPQDLKLPT APEKPIIVTT QDARPQVFFD
     RWAGNPPGMS VVVGRLKQVN PRTIRFVSLI HNTVRGAAGG GVLTAELLVE KGYIDKR