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Protein

Urease subunit alpha

Gene

ureC

Organism
Prochlorococcus marinus subsp. pastoris (strain PCC 9511)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.UniRule annotation1 Publication

Cofactori

Ni cationUniRule annotationNote: Binds 2 nickel ions per subunit.UniRule annotation

Enzyme regulationi

Inhibited by HgCl2 and acetohydroxyamic acid slightly by EDTA, but not by boric acid or L-methionine-DL-sulfoximine.1 Publication

Kineticsi

  1. KM=0.23 mM for urea1 Publication
  1. Vmax=0.095 mmol/min/mg enzyme1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius.1 Publication

Pathwayi: urea degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and NH(3) from urea (urease route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Urease subunit alpha (ureC), Urease subunit gamma (ureA)
This subpathway is part of the pathway urea degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and NH(3) from urea (urease route), the pathway urea degradation and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi136 – 1361Nickel 1; via tele nitrogenUniRule annotation
Metal bindingi138 – 1381Nickel 1; via tele nitrogenUniRule annotation
Metal bindingi219 – 2191Nickel 1; via carbamate groupUniRule annotation
Metal bindingi219 – 2191Nickel 2; via carbamate groupUniRule annotation
Binding sitei221 – 2211SubstrateUniRule annotation
Metal bindingi248 – 2481Nickel 2; via pros nitrogenUniRule annotation
Metal bindingi274 – 2741Nickel 2; via tele nitrogenUniRule annotation
Active sitei322 – 3221Proton donorUniRule annotation
Metal bindingi362 – 3621Nickel 1UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.

Protein family/group databases

MEROPSiM38.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Urease subunit alphaUniRule annotation (EC:3.5.1.5UniRule annotation)
Alternative name(s):
Urea amidohydrolase subunit alphaUniRule annotation
Gene namesi
Name:ureCUniRule annotation
OrganismiProchlorococcus marinus subsp. pastoris (strain PCC 9511)
Taxonomic identifieri100363 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 569569Urease subunit alphaPRO_0000234165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191N6-carboxylysineUniRule annotation

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two nickel ions.UniRule annotation

Interactioni

Subunit structurei

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Two heterotrimers associate to form the active enzyme. In most bacteria it is thought that three heterotrimers form the active enzyme.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9L644.
SMRiQ9L644. Positions 5-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini131 – 569439UreaseUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the urease family.UniRule annotation
Contains 1 urease domain.UniRule annotation

Family and domain databases

CDDicd00375. Urease_alpha. 1 hit.
Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
InterProiIPR006680. Amidohydro-rel.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
IPR011612. Urease_alpha_N_dom.
IPR017950. Urease_AS.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSiPR01752. UREASE.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 2 hits.
TIGRFAMsiTIGR01792. urease_alph. 1 hit.
PROSITEiPS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9L644-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYKINRKTY AQTYGPTKGD RVRLADTELI IEVEKDFTTY GDEVKFGGGK
60 70 80 90 100
VIRDGMGQSQ VTREDGAVDT VITNALIVDW WGIVKADVGL KDGKIYEIGK
110 120 130 140 150
AGNPDIQDNI NIIIGSSTEV IAGEGHILTA GSIDTHIHFI CPQQIETALA
160 170 180 190 200
SGVTTMLGGG TGPATGTNAT TCTPGAFHIS RMIQSAEAFP VNLGFFGKGN
210 220 230 240 250
SSNETNLFEQ VNAGACGLKL HEDWGTTPST INSCLNVADT LDVQVCIHTD
260 270 280 290 300
TLNEAGFVED TIAAIAGRTI HTFHTEGAGG GHAPDIIKIC GENNVLPSST
310 320 330 340 350
NPTRPYTKNT LEEHLDMLMV CHHLDSKIPE DIAFAESRIR RETIAAEDIL
360 370 380 390 400
HDIGAFSIIA SDSQAMGRVG EVITRTFQTA HKMKVQRGPL PEDSDRNDNY
410 420 430 440 450
RVKRYISKVT INPAIAHGIN RFVGSIEKGK IADLVLWKPS FFGVKPELVV
460 470 480 490 500
KGGSIVWSQM GDANASIPTP GPVHGRPMFA NYGQSLLKSS FTFLSKNAIE
510 520 530 540 550
LDIPNKLSLQ KNCLAVENTR SINKLDLKLN NKLPNITVDP QTYEVFADGV
560
LLSCEPLEEV PMAQKYFLL
Length:569
Mass (Da):61,653
Last modified:October 1, 2000 - v1
Checksum:iBA01CA894931C487
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF242489 Genomic DNA. Translation: AAF70248.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF242489 Genomic DNA. Translation: AAF70248.1.

3D structure databases

ProteinModelPortaliQ9L644.
SMRiQ9L644. Positions 5-569.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM38.982.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.

Family and domain databases

CDDicd00375. Urease_alpha. 1 hit.
Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
InterProiIPR006680. Amidohydro-rel.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
IPR011612. Urease_alpha_N_dom.
IPR017950. Urease_AS.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSiPR01752. UREASE.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 2 hits.
TIGRFAMsiTIGR01792. urease_alph. 1 hit.
PROSITEiPS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiURE1_PROS9
AccessioniPrimary (citable) accession number: Q9L644
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 1, 2000
Last modified: September 7, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.