MCR_SULTO
ID MCR_SULTO Reviewed; 359 AA.
AC Q96YK1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Malonyl-CoA reductase;
DE EC=1.2.1.75;
GN Name=mcr; Synonyms=scr; OrderedLocusNames=STK_21710;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION AS A MALONYL COA REDUCTASE, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, RNA BINDING,
RP NOMENCLATURE, AND CATALYTIC ACTIVITY.
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. Can also use succinyl-CoA
CC and succinate semialdehyde as substrates but at a lower rate than
CC malonyl-CoA. {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 Evidence={ECO:0000269|PubMed:17041055};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17041055};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17041055};
CC Note=Divalent metal cations such as Mg(2+) and Mn(2+) ions at 5 mM.
CC {ECO:0000269|PubMed:17041055};
CC -!- ACTIVITY REGULATION: Activated by dithioerythritol (5 mM) and inhibited
CC by the thiol-blocking agent iodoacetamide (0.1 mM).
CC {ECO:0000269|PubMed:17041055}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for NADP (with 0.2 mM malonyl-CoA)
CC {ECO:0000269|PubMed:17041055};
CC KM=40 uM for malonyl-CoA (with 0.5 mM NADP)
CC {ECO:0000269|PubMed:17041055};
CC pH dependence:
CC Optimum pH is 7.2, with half-maximal activities at pH 6 and 8.
CC {ECO:0000269|PubMed:17041055};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:17041055};
CC -!- SUBUNIT: Homodimer and possibly a tetramer.
CC {ECO:0000269|PubMed:17041055}.
CC -!- MISCELLANEOUS: This enzyme contains bound RNA, but the physiological
CC role is not known. {ECO:0000305|PubMed:17041055}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BA000023; BAB67276.1; -; Genomic_DNA.
DR PDB; 4DPK; X-ray; 2.05 A; A/B/C/D=1-359.
DR PDB; 4DPL; X-ray; 1.90 A; A/B/C/D=1-359.
DR PDB; 4DPM; X-ray; 2.30 A; A/B/C/D/E/F=1-359.
DR PDBsum; 4DPK; -.
DR PDBsum; 4DPL; -.
DR PDBsum; 4DPM; -.
DR AlphaFoldDB; Q96YK1; -.
DR SMR; Q96YK1; -.
DR STRING; 273063.STK_21710; -.
DR EnsemblBacteria; BAB67276; BAB67276; STK_21710.
DR KEGG; sto:STK_21710; -.
DR PATRIC; fig|273063.9.peg.2464; -.
DR eggNOG; arCOG00494; Archaea.
DR OMA; CEEEMKM; -.
DR BioCyc; MetaCyc:MON-13611; -.
DR BRENDA; 1.2.1.75; 15396.
DR Proteomes; UP000001015; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 3D-structure; NADP; Oxidoreductase; Reference proteome; RNA-binding.
FT CHAIN 1..359
FT /note="Malonyl-CoA reductase"
FT /id="PRO_0000418855"
FT ACT_SITE 153
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 16..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 183..184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 335..336
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4DPL"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 31..41
FT /evidence="ECO:0007829|PDB:4DPL"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:4DPL"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:4DPL"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:4DPL"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 153..168
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:4DPL"
FT TURN 307..311
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 313..323
FT /evidence="ECO:0007829|PDB:4DPL"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:4DPL"
FT TURN 335..340
FT /evidence="ECO:0007829|PDB:4DPL"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:4DPL"
SQ SEQUENCE 359 AA; 39560 MW; 426AAE51597DD0E8 CRC64;
MILMRRTLKA AILGATGLVG IEYVRMLSNH PYIKPAYLAG KGSVGKPYGE VVRWQTVGQV
PKEIADMEIK PTDPKLMDDV DIIFSPLPQG AAGPVEEQFA KEGFPVISNS PDHRFDPDVP
LLVPELNPHT ISLIDEQRKR REWKGFIVTT PLCTAQGAAI PLGAIFKDYK MDGAFITTIQ
SLSGAGYPGI PSLDVVDNIL PLGDGYDAKT IKEIFRILSE VKRNVDEPKL EDVSLAATTH
RIATIHGHYE VLYVSFKEET AAEKVKETLE NFRGEPQDLK LPTAPSKPII VMNEDTRPQV
YFDRWAGDIP GMSVVVGRLK QVNKRMIRLV SLIHNTVRGA AGGGILAAEL LVEKGYIEK
