P44391 (URE1_HAEIN) Reviewed, UniProtKB/Swiss-Prot

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:	HI_0539

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
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. HAMAP MF_01953
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 HAMAP MF_01953.
Post-translational modification	Carbamylation allows a single lysine to coordinate two nickel ions By similarity. HAMAP MF_01953
Sequence similarities	Belongs to the urease family. Contains 1 urease domain.

Ontologies

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 572	572	Urease subunit alpha HAMAP MF_01953		PRO_0000067542
Regions
	Domain	136 – 572	437	Urease
Sites
	Active site	327	1	Proton donor By similarity
	Metal binding	141	1	Nickel 2 By similarity
	Metal binding	143	1	Nickel 2 By similarity
	Metal binding	224	1	Nickel 1; via carbamate group By similarity
	Metal binding	224	1	Nickel 2; via carbamate group By similarity
	Metal binding	253	1	Nickel 1 By similarity
	Metal binding	279	1	Nickel 1 By similarity
	Metal binding	367	1	Nickel 2 By similarity
	Binding site	226	1	Substrate By similarity
Amino acid modifications
	Modified residue	224	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44391 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 5E26396652BB6B43	FASTA	572	61,776
	10 20 30 40 50 60 MALTISRAQY VATYGPTVGD KVRLGDTNLW ATIEQDLLTK GDECKFGGGK SVRDGMAQSG 70 80 90 100 110 120 TATRDNPNVL DFVITNVMII DAKLGIIKAD IGIRDGRIVG IGQAGNPDTM DNVTPNMIIG 130 140 150 160 170 180 ASTEVHNGAH LIATAGGIDT HIHFICPQQA QHAIESGVTT LIGGGTGPAD GTHATTCTPG 190 200 210 220 230 240 AWYMERMFQA AEALPVNVGF FGKGNCSTLD PLREQIEAGA LGLKIHEDWG ATPAVIDSAL 250 260 270 280 290 300 KVADEMDIQV AIHTDTLNES GFLEDTMKAI DGRVIHTFHT EGAGGGHAPD IIKAAMYSNV 310 320 330 340 350 360 LPASTNPTRP FTKNTIDEHL DMLMVCHHLD KRVPEDVAFA DSRIRPETIA AEDILHDMGV 370 380 390 400 410 420 FSIMSSDSQA MGRIGEVVIR TWQTADKMKM QRGELGNEGN DNFRIKRYIA KYTINPAIAH 430 440 450 460 470 480 GIAEHIGSLE VGKIADIVLW KPMFFGVKPE VVIKKGFISY AKMGDPNASI PTPQPVFYRP 490 500 510 520 530 540 MYGAQGLATA QTAVFFVSQA AEKADIRAKF GLHKETIAVK GCRNVGKKDL VHNDVTPNIT 550 560 570 VDAERYEVRV DGELITCEPV DSVPLGQRYF LF

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22197.1.
PIR	H64075.
RefSeq	NP_438697.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P44391.
SMR	P44391. Positions 5-572.
ModBase	Search...
Protein family/group databases
MEROPS	M38.982.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	950768.
GenomeReviews	Gene locus HI_0539 in contig L42023_GR.
KEGG	hin:HI0539.
NMPDR	fig|71421.1.peg.510.
PATRIC	20189631. VBIHaeInf48452_0558.
TIGR	HI_0539.
Phylogenomic databases
HOGENOM	HBG357507.
OMA	TIHAFHT.
ProtClustDB	PRK13207.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0539-MONOMER.
Family and domain databases
HAMAP	MF_01953. Urease_alpha. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR011059. Metal-dep_hydrolase_composite. IPR011612. Urease_alpha_N. IPR005848. Urease_asu. IPR017951. Urease_asu_c. IPR017950. Urease_asu_CS. [Graphical view]
KO	K01428.
Pfam	PF01979. Amidohydro_1. 1 hit. PF00449. Urease_alpha. 1 hit. [Graphical view]
PRINTS	PR01752. UREASE.
SUPFAM	SSF51338. Metalo_hydrolase. 2 hits.
TIGRFAMs	TIGR01792. Urease_alph. 1 hit.
PROSITE	PS01120. UREASE_1. 1 hit. PS00145. UREASE_2. 1 hit. PS51368. UREASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

URE1_HAEIN

Accession

Primary (citable) accession number: P44391

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program