Q96YK1 (MCR_SULTO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malonyl-CoA reductase
EC=1.2.1.75

Gene names

Name:	mcr
Synonyms:	scr
Ordered Locus Names:	STK_21710

Organism

Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) [Complete proteome] [HAMAP]

Taxonomic identifier

273063 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus › Sulfolobus tokodaii

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. Can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA. Ref.2
Catalytic activity	Malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH. Ref.2
Cofactor	Divalent cations such as magnesium or manganese ions at 5 mM. Ref.2
Enzyme regulation	Activated by dithioerythritol (5 mM) and inhibited by the thiol-blocking agent iodoacetamide (0.1 mM). Ref.2
Subunit structure	Homodimer and possibly a tetramer. Ref.2
Miscellaneous	This enzyme contains bound RNA, but the physiological role is not known (Ref.2).
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=25 µM for NADP (with 0.2 mM malonyl-CoA) Ref.2 KM=40 µM for malonyl-CoA (with 0.5 mM NADP) pH dependence: Optimum pH is 7.2, with half-maximal activities at pH 6 and 8. Temperature dependence: Optimum temperature is 85 degrees Celsius.

Ontologies

Keywords
Ligand	NADP RNA-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	aspartate metabolic process Inferred from electronic annotation. Source: InterPro isoleucine biosynthetic process Inferred from electronic annotation. Source: InterPro lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: InterPro methionine biosynthetic process Inferred from electronic annotation. Source: InterPro threonine biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW aspartate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 359

359

Malonyl-CoA reductase

PRO_0000418855

Regions

Nucleotide binding

16 – 19

4

NADP By similarity

Nucleotide binding

183 – 184

2

NADP By similarity

Nucleotide binding

335 – 336

2

NADP By similarity

Sites

Active site

153

1

Acyl-thioester intermediate By similarity

Active site

248

1

Proton acceptor By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

359

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Turn

13 – 16

4

Helix

20 – 28

9

Beta strand

31 – 41

11

Turn

42 – 45

4

Helix

48 – 51

4

Beta strand

56 – 58

3

Helix

62 – 65

4

Helix

74 – 76

3

Beta strand

82 – 85

4

Turn

89 – 91

3

Helix

92 – 101

10

Beta strand

105 – 108

4

Turn

112 – 115

4

Turn

124 – 126

3

Helix

128 – 132

5

Helix

133 – 141

9

Beta strand

144 – 149

6

Helix

153 – 168

16

Beta strand

171 – 180

10

Helix

182 – 185

4

Helix

192 – 195

4

Helix

204 – 218

15

Helix

230 – 232

3

Beta strand

234 – 238

5

Beta strand

248 – 258

11

Helix

262 – 270

9

Helix

275 – 278

4

Beta strand

288 – 292

5

Helix

300 – 303

4

Turn

307 – 311

5

Beta strand

313 – 323

11

Beta strand

326 – 333

8

Turn

335 – 340

6

Helix

341 – 353

13

Sequences

	Sequence		Length	Mass (Da)
	Q96YK1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 426AAE51597DD0E8	FASTA	359	39,560
	10 20 30 40 50 60 MILMRRTLKA AILGATGLVG IEYVRMLSNH PYIKPAYLAG KGSVGKPYGE VVRWQTVGQV 70 80 90 100 110 120 PKEIADMEIK PTDPKLMDDV DIIFSPLPQG AAGPVEEQFA KEGFPVISNS PDHRFDPDVP 130 140 150 160 170 180 LLVPELNPHT ISLIDEQRKR REWKGFIVTT PLCTAQGAAI PLGAIFKDYK MDGAFITTIQ 190 200 210 220 230 240 SLSGAGYPGI PSLDVVDNIL PLGDGYDAKT IKEIFRILSE VKRNVDEPKL EDVSLAATTH 250 260 270 280 290 300 RIATIHGHYE VLYVSFKEET AAEKVKETLE NFRGEPQDLK LPTAPSKPII VMNEDTRPQV 310 320 330 340 350 YFDRWAGDIP GMSVVVGRLK QVNKRMIRLV SLIHNTVRGA AGGGILAAEL LVEKGYIEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7." Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H. DNA Res. 8:123-140(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.
[2]	"Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp." Alber B., Olinger M., Rieder A., Kockelkorn D., Jobst B., Hugler M., Fuchs G. J. Bacteriol. 188:8551-8559(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A MALONYL COA REDUCTASE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, RNA BINDING, NOMENCLATURE, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000023 Genomic DNA. Translation: BAB67276.1.

RefSeq

NP_378167.1. NC_003106.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DPK	X-ray	2.05	A/B/C/D	1-359	[»]
4DPL	X-ray	1.90	A/B/C/D	1-359	[»]
4DPM	X-ray	2.30	A/B/C/D/E/F	1-359	[»]

ProteinModelPortal

Q96YK1.

ModBase

Search...

Protein-protein interaction databases

STRING

273063.ST2171.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAB67276; BAB67276; STK_21710.

GeneID

1460244.

KEGG

sto:ST2171.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0136.

HOGENOM

HOG000013358.

KO

K15017.

OMA

VEEQFAK.

ProtClustDB

PRK08664.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13611.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR005676. Asp_semi-ald_DH_pep-lack.
IPR012080. Asp_semialdehyde_DH.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
[Graphical view]

Pfam

PF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]

PIRSF

PIRSF000148. ASA_dh. 1 hit.

SMART

SM00859. Semialdhyde_dh. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00978. asd_EA. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MCR_SULTO

Accession

Primary (citable) accession number: Q96YK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2012
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program