Reviewed, UniProtKB/Swiss-Prot Q57872 (DCD_METJA)

Names and origin

Protein names

Recommended name:
    dCTP deaminase, dUMP-forming
    EC=3.5.4.30
Alternative name(s):
    Bifunctional deaminase/diphosphatase
    MjDCD-DUT
      Short name=DCD/DUT

Gene names

Name:	dcd
Ordered Locus Names:	MJ0430

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes two consecutive reactions to form dUMP using dCTP as substrate. HAMAP MF_00146
Catalytic activity	dCTP + 2 H2O = dUMP + diphosphate + NH3. HAMAP MF_00146
Cofactor	Magnesium. HAMAP MF_00146
Enzyme regulation	Inhibited by dTTP. HAMAP MF_00146
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1. HAMAP MF_00146
Subunit structure	Homohexamer. HAMAP MF_00146
Sequence similarities	Belongs to the dCTP deaminase family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.5. HAMAP MF_00146 Temperature dependence: Retains over 70% of its activity after heating at 90 degrees Celsius for 10 min.
Mass spectrometry	Molecular mass is 23619±94 Da from positions 1 - 204. Determined by MALDI. Ref.3

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	dUTP biosynthetic process Inferred from electronic annotation. Source: InterPro pyrimidine ribonucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	dCTP deaminase (dUMP-forming) activity Inferred from electronic annotation. Source: EC dCTP deaminase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 204

204

dCTP deaminase, dUMP-forming HAMAP MF_00146

PRO_0000156029

Experimental info

Mutagenesis

135

1

D → N: Loss of activity. Ref.3

Mutagenesis

145

1

E → Q: Loss of dCTP deaminase activity, but retains 25% dUTP pyrophosphatase activity. Ref.3

Secondary structure

1

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204

Helix Strand Turn

Details...

Helix

5 – 13

9

Beta strand

16 – 21

6

Helix

24 – 26

3

Beta strand

32 – 36

5

Beta strand

38 – 43

6

Beta strand

46 – 48

3

Beta strand

56 – 60

5

Beta strand

62 – 68

7

Helix

76 – 86

11

Beta strand

89 – 94

6

Beta strand

96 – 105

10

Beta strand

110 – 116

7

Helix

118 – 121

4

Turn

122 – 124

3

Beta strand

125 – 127

3

Beta strand

139 – 151

13

Beta strand

153 – 156

4

Beta strand

160 – 171

12

Helix

196 – 198

3

Sequences

	Sequence		Length	Mass (Da)
	Q57872-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 1218368057723371	FASTA	204	23,432
	10 20 30 40 50 60 MILSDKDIID YVTSKRIIIK PFNKDFVGPC SYDVTLGDEF IIYDDEVYDL SKELNYKRIK 70 80 90 100 110 120 IKNSILVCPL NYNLTEEKIN YFKEKYNVDY VVEGGVLGTT NEYIELPNDI SAQYQGRSSL 130 140 150 160 170 180 GRVFLTSHQT AGWIDAGFKG KITLEIVAFD KPVILYKNQR IGQLIFSKLL SPADVGYSER 190 200 KTSKYAYQKS VMPSLIHLDN HKKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii." Bjoernberg O., Neuhard J., Nyman P.O. J. Biol. Chem. 278:20667-20672(2003) [PubMed: 12670946] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION.
[3]	"The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase." Li H., Xu H., Graham D.E., White R.H. J. Biol. Chem. 278:11100-11106(2003) [PubMed: 12538648] [Abstract] Cited for: CHARACTERIZATION, MASS SPECTROMETRY, MUTAGENESIS OF ASP-135 AND GLU-145.
[4]	"Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases." Johansson E., Bjoernberg O., Nyman P.O., Larsen S. J. Biol. Chem. 278:27916-27922(2003) [PubMed: 12756253] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 30-204.
[5]	"Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii." Huffman J.L., Li H., White R.H., Tainer J.A. J. Mol. Biol. 331:885-896(2003) [PubMed: 12909016] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 23-204.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L77117 Genomic DNA. Translation: AAB98415.1.

PIR

F64353.

RefSeq

NP_247404.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OGH	X-ray	1.88	A/B	1-204	[»]
1PKH	X-ray	1.42	A/B	1-204	[»]
1PKJ	X-ray	2.10	A/B	1-204	[»]
1PKK	X-ray	1.77	A/B	1-204	[»]
2HXB	X-ray	2.55	A	1-204	[»]
2HXD	X-ray	2.30	A	1-204	[»]
3GF0	X-ray	2.62	A	1-204	[»]

ModBase

Search...

Genome annotation databases

GeneID

1451290.

GenomeReviews

Gene locus MJ0430 in contig L77117_GR.

KEGG

mja:MJ0430.

NMPDR

fig|243232.1.peg.441.

TIGR

MJ0430.

Phylogenomic databases

HOGENOM

Q57872.

OMA

Q57872. ITLEIVA.

Enzyme and pathway databases

BioCyc

MJAN243232:MJ_0430-MON.

Family and domain databases

HAMAP

MF_00146. Divergent sequence.
[Tree]

InterPro

IPR011962. dCTP_deam.
[Graphical view]

ProDom

PD004900. dCTP_deaminase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR02274. dCTP_deam. 1 hit.

ProtoNet

Search...

Entry information

Entry name

DCD_METJA

Accession

Primary (citable) accession number: Q57872

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)