Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q1B9W4 (Q1B9W4_MYCSS) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 50. Feed History...

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

Names and origin

Protein namesRecommended name:
Uroporphyrinogen decarboxylase HAMAP MF_00218
Short name=UPD HAMAP MF_00218
Short name=URO-D HAMAP MF_00218
EC=4.1.1.37 HAMAP MF_00218
Gene names
Name:hemE HAMAP MF_00218
Ordered Locus Names:Mmcs_2212
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III By similarity. HAMAP MF_00218 SAAS SAAS006361

Catalytic activity

Uroporphyrinogen III = coproporphyrinogen + 4 CO2. HAMAP MF_00218 RuleBase RU000554 SAAS SAAS006361

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen III from 5-aminolevulinate: step 4/4. RuleBase RU000554

Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. HAMAP MF_00218 SAAS SAAS006361

Subunit structure

Homodimer By similarity. HAMAP MF_00218 SAAS SAAS006361

Subcellular location

Cytoplasm By similarity HAMAP MF_00218 SAAS SAAS006361.

Sequence similarities

Belongs to the uroporphyrinogen decarboxylase family. HAMAP MF_00218 RuleBase RU004169

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region48 – 525Substrate binding By similarity HAMAP MF_00218

Sites

Binding site971Substrate By similarity HAMAP MF_00218
Binding site1721Substrate By similarity HAMAP MF_00218
Binding site2271Substrate By similarity HAMAP MF_00218
Binding site3511Substrate By similarity HAMAP MF_00218
Site971Transition state stabilizer By similarity HAMAP MF_00218

Sequences

Sequence LengthMass (Da)Tools
Q1B9W4 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: CC8F219ABCE28FA2

FASTA37239,208
        10         20         30         40         50         60 
MVIRASAAPL PVVAALGAMN TRRELPDSPY LAAARGRKPA RVPVWFMRQA GRSLPEYRAL 

        70         80         90        100        110        120 
RARNTMMQAC FDADLITEIT LQPVRRHGVD AAILFSDIVV PLRASGIALD IVPDVGPVID 

       130        140        150        160        170        180 
HPVRTAADVA AIRPLERQTV EPVEQAVRML TAALGDVPLI GFAGAPFTLA SYLVEGGPSK 

       190        200        210        220        230        240 
HHEHTKAMML GAPDTWHALM SALTDVTIAF LQAQVDAGVD AIQVFDSWAG TLSLADYRAY 

       250        260        270        280        290        300 
VLPHSARVFQ ALAPAGVPMT HFGVGTAELL GAMSEAIATS GAPGVVGVDW RTSLTDAAGR 

       310        320        330        340        350        360 
VERGSALQGN LDPVVLLAGW PVVERAVRAV VEDGRRAVDA GAAGHVFNLG HGVLPATDPE 

       370 
IVTATVELVH SL

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. MCS."
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., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000384 Genomic DNA. Translation: ABG08320.1.
RefSeqYP_639376.1. NC_008146.1.

3D structure databases

ProteinModelPortalQ1B9W4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1B9W4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000062135; EBMYCP00000060302; EBMYCG00000062130.
GeneID4111045.
GenomeReviewsGene locus Mmcs_2212 in contig CP000384_GR.
KEGGmmc:Mmcs_2212.
PATRIC18114622. VBIMycSp106721_2264.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
GeneTreeEBGT00050000016469.
HOGENOMHBG628392.
OMAPRIHFGV.
ProtClustDBPRK00115.

Family and domain databases

HAMAPMF_00218. URO_D.
[Tree]
InterProIPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]
KOK01599.
PANTHERPTHR21091:SF2. HemE. 1 hit.
PfamPF01208. URO-D. 1 hit.
[Graphical view]
TIGRFAMsTIGR01464. HemE. 1 hit.
PROSITEPS00906. UROD_1. 1 hit.
PS00907. UROD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ1B9W4_MYCSS
AccessionPrimary (citable) accession number: Q1B9W4
Entry history
Integrated into UniProtKB/TrEMBL: July 11, 2006
Last sequence update: July 11, 2006
Last modified: December 14, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info