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Q68WR3 (HEM3_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Porphobilinogen deaminase

Short name=PBG
EC=2.5.1.61
Alternative name(s):
Hydroxymethylbilane synthase
Short name=HMBS
Pre-uroporphyrinogen synthase
Gene names
Name:hemC
Ordered Locus Names:RT0453
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps By similarity. HAMAP-Rule MF_00260

Catalytic activity

4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH3. HAMAP-Rule MF_00260

Cofactor

Binds 1 dipyrromethane group covalently By similarity. HAMAP-Rule MF_00260

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. HAMAP-Rule MF_00260

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00260

Miscellaneous

The porphobilinogen subunits are added to the dipyrromethane group By similarity.

Sequence similarities

Belongs to the HMBS family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpeptidyl-pyrromethane cofactor linkage

Inferred from electronic annotation. Source: InterPro

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionhydroxymethylbilane synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Porphobilinogen deaminase HAMAP-Rule MF_00260
PRO_0000142983

Amino acid modifications

Modified residue2421S-(dipyrrolylmethanemethyl)cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q68WR3 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 0DC81A31938FAABE

FASTA29933,561
        10         20         30         40         50         60 
MINSIRIGTR NSTLALIQTN LVIAQIKQFF PDINCEIVPI ITSGDLIQNK PLYDIGGKAL 

        70         80         90        100        110        120 
FLKEIEQALL DKKIDLAVHS LKDIPGRIPV DLVIAAVLER EDPRDVLVCL NYKSIETLPQ 

       130        140        150        160        170        180 
NAVIGSSAVR RKAFIKKIRP DLNIKVFRGN VDSRIKKLMT GEVDATILSY AGLKRLNAFN 

       190        200        210        220        230        240 
KKYCHLIEYS QILPCVGQGV IAVEIRKDDN AMFNICNQIN HIPTFELIKP ERAFLEHLDA 

       250        260        270        280        290 
NCSTPIGAYS QYLDAYNIQT DFMLGKLDCN KIIFQTEITN INTSRECGIK AAKMMLAQQ 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU03929.1.
RefSeqYP_067411.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68WR3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257363.RT0453.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU03929; AAU03929; RT0453.
GeneID2959104.
KEGGrty:RT0453.
PATRIC17910146. VBIRicTyp34752_0484.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0181.
HOGENOMHOG000228587.
KOK01749.
OMAPLRGNAN.
OrthoDBEOG6HB9Z6.
ProtClustDBPRK00072.

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-475-MONOMER.
UniPathwayUPA00251; UER00319.

Family and domain databases

Gene3D3.30.160.40. 1 hit.
HAMAPMF_00260. Porphobil_deam.
InterProIPR000860. 4pyrrol_synth_OHMeBilane_synth.
IPR022419. Porphobilin_deaminase_cofac_BS.
IPR022417. Porphobilin_deaminase_N.
IPR022418. Porphobilinogen_deaminase_C.
[Graphical view]
PANTHERPTHR11557. PTHR11557. 1 hit.
PfamPF01379. Porphobil_deam. 1 hit.
PF03900. Porphobil_deamC. 1 hit.
[Graphical view]
PIRSFPIRSF001438. 4pyrrol_synth_OHMeBilane_synth. 1 hit.
PRINTSPR00151. PORPHBDMNASE.
SUPFAMSSF54782. SSF54782. 1 hit.
TIGRFAMsTIGR00212. hemC. 1 hit.
PROSITEPS00533. PORPHOBILINOGEN_DEAM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM3_RICTY
AccessionPrimary (citable) accession number: Q68WR3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways