Reviewed, UniProtKB/Swiss-Prot A4XMA9 (URE1_CALS8)

Names and origin

Protein names

Recommended name:
    Urease subunit alpha
    EC=3.5.1.5
Alternative name(s):
    Urea amidohydrolase subunit alpha

Gene names

Name:	ureC
Ordered Locus Names:	Csac_2467

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	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953
Cofactor	Binds 2 nickel ions per subunit By similarity.
Pathway	Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP MF_01953
Subunit structure	Heterotrimer of ureA (gamma), ureB (beta) and ureC (alpha) subunits. Three heterotrimers associate to form the active enzyme By similarity.
Subcellular location	Cytoplasm By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two nickel ions By similarity.
Sequence similarities	Belongs to the urease family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Nickel
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	urea metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW urease activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 570	570	Urease subunit alpha HAMAP MF_01953		PRO_1000088487
Sites
	Active site	324	1	Proton donor By similarity
	Metal binding	138	1	Nickel 2 By similarity
	Metal binding	140	1	Nickel 2 By similarity
	Metal binding	221	1	Nickel 1; via carbamate group By similarity
	Metal binding	221	1	Nickel 2; via carbamate group By similarity
	Metal binding	250	1	Nickel 1 By similarity
	Metal binding	276	1	Nickel 1 By similarity
	Metal binding	364	1	Nickel 2 By similarity
	Binding site	223	1	Substrate By similarity
Amino acid modifications
	Modified residue	221	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4XMA9-1 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: BD775C59117A9D20	FASTA	570	62,664
	10 20 30 40 50 60 MAYHIKREDY VKIYGPTVGD KIRLADTDLI IEIEKDYTVY GEECKFGAGK NIRDGMSQNQ 70 80 90 100 110 120 FACNNSALDI VITNVVIIDW WGIVKGDIGI KDGKIVGIGK AGNPNVMDGV TPNMVIGPST 130 140 150 160 170 180 DVISGEGLIA TAGAIDTHVH FICPQQIETA LYKGITTLIG GGIGPTEGTK ATTCTPGAWN 190 200 210 220 230 240 IFKMLKAVDN FPVNIGLTGK GNSSYEKPLI EQVKAGVVGF KIHEDWGATP TVIDTCLKVA 250 260 270 280 290 300 DEFDVQVALH TDSMNEAGFV EDTIKAIGNR VLHAYHVEGA GGGHAPDVLK VVQYKNIIPS 310 320 330 340 350 360 STTPTMPHTI NTFSEHLDML IFCHHLDKNL EEDVEFAKAR IRETTMAAED YLHDIGAISI 370 380 390 400 410 420 INSDSQAMGR IGEVITRTWQ TADKMKKIYG RLPEDTQNDN YRVKRYISKY TINPAIAHGI 430 440 450 460 470 480 SQYIGSLEPG KIADIVLWKP AFFGVKPEMI IKGGFIIASK MGDANASIPT PQPVIMKKMF 490 500 510 520 530 540 GAFGKAVYDT AVTFVSGYFY ENEINKKIGI NKKVLPVKNC RNISKENMIY NNQLPKIEID 550 560 570 YKTFEVFVNG NKINVPPAVS LNMTRRYNLF

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000679 Genomic DNA. Translation: ABP68044.1.
RefSeq	YP_001181235.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A4XMA9.
Genome annotation databases
GeneID	5088293.
GenomeReviews	Gene locus Csac_2467 in contig CP000679_GR.
KEGG	csc:Csac_2467.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	SHIHFIC.
Family and domain databases
HAMAP	MF_01953. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR011612. Urease_alpha_N. IPR005848. Urease_asu. IPR017951. Urease_asu_c. IPR017952. Urease_asu_core. IPR017950. Urease_asu_CS. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. PF00449. Urease_alpha. 1 hit. [Graphical view]
PRINTS	PR01752. UREASE.
TIGRFAMs	TIGR01792. urease_alph. 1 hit.
PROSITE	PS01120. UREASE_1. 1 hit. PS00145. UREASE_2. False negative. PS51368. UREASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

URE1_CALS8

Accession

Primary (citable) accession number: A4XMA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 29, 2007
Last modified:	November 3, 2009
This is version 22 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)