A4XKT2 (PYRC_CALS8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	Csac_1932

Organism

Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]

Taxonomic identifier

351627 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220_B
Cofactor	Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220_B
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220_B
Subunit structure	Homodimer By similarity. HAMAP MF_00220_B
Sequence similarities	Belongs to the DHOase family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dihydroorotase activity Inferred from electronic annotation. Source: EC metal 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 – 430	430	Dihydroorotase HAMAP MF_00220_B		PRO_0000325590
Sites
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	63	1	Zinc 1 By similarity
	Metal binding	143	1	Zinc 1; via carbamate group By similarity
	Metal binding	143	1	Zinc 2; via carbamate group By similarity
	Metal binding	180	1	Zinc 2 By similarity
	Metal binding	233	1	Zinc 2 By similarity
	Metal binding	306	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	143	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4XKT2 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: 75C5C16A7ED4318E	FASTA	430	47,394
	10 20 30 40 50 60 MILIKNAQII NSLHDKVEKA DILIVDDKIK KIGKDIEENP EKMTIIDASG KVVMPSFTDI 70 80 90 100 110 120 HCHLREPGFE YKEDIKSGSR SAAAGGFTTI CCMPNTNPPV DNRAMVAYIK YRAREVSPIE 130 140 150 160 170 180 VLPVGAITKG LLGEELAEIG FMKEEGAIAI SDDGKCVMNA NLMKNALLYS RDFSIPVISH 190 200 210 220 230 240 CEDTNLSEGG QINLGYVSTI TGLRGIPREA ESVIIARDIL LAKETKSHLH ITHVSTKESV 250 260 270 280 290 300 RLIKMAKEWG VNVTADTCPH YISLTEEEVL GFNTNAKVNP PLRTQEDVEA LIEGLKEGVI 310 320 330 340 350 360 DCISTDHAPH HKDEKNVEFN LAASGTIGFE TAFSVLFTYL VEKNGFDIGK IVELLNHNPR 370 380 390 400 410 420 KIIGLSPNVL KEGEKANLVI VDLKKKWEVK EENIVSKSKN SVFLGKLLTS YVETVIYNGK 430 ILKKDGVLNC

References

[1]

"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000679 Genomic DNA. Translation: ABP67517.1.
RefSeq	YP_001180708.1. NC_009437.1.
3D structure databases
ProteinModelPortal	A4XKT2.
ModBase	Search...
Protein-protein interaction databases
STRING	A4XKT2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5089294.
GenomeReviews	Gene locus Csac_1932 in contig CP000679_GR.
KEGG	csc:Csac_1932.
PATRIC	21253612. VBICalSac56748_2112.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HBG724623.
OMA	SHHQPHE.
ProtClustDB	CLSK2473347.
Family and domain databases
HAMAP	MF_00220_B. PyrC_type2_B. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR004722. DHOase. IPR002195. Dihydroorotase_CS. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
KO	K01465.
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR00857. PyrC_multi. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. False negative. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRC_CALS8

Accession

Primary (citable) accession number: A4XKT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	May 29, 2007
Last modified:	December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program