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Q57BW7 (HEM6_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:
Coproporphyrinogen-III oxidase, aerobic

Short name=Coprogen oxidase
Short name=Coproporphyrinogenase
EC=1.3.3.3
Gene names
Name:hemF
Ordered Locus Names:BruAb1_1539
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III By similarity. HAMAP MF_00333

Catalytic activity

Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O. HAMAP MF_00333

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1. HAMAP MF_00333

Subunit structure

Homodimer By similarity. HAMAP MF_00333

Subcellular location

Cytoplasm By similarity HAMAP MF_00333.

Sequence similarities

Belongs to the aerobic coproporphyrinogen-III oxidase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processporphyrin-containing compound biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncoproporphyrinogen oxidase activity

Inferred from electronic annotation. Source: EC

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
PRO_1000119788

Regions

Region72 – 8110Important for dimerization By similarity
Region132 – 1343Substrate binding By similarity
Region268 – 30336Important for dimerization By similarity
Region286 – 2916Substrate binding By similarity

Sites

Active site1301Proton donor By similarity
Binding site1161Substrate By similarity
Site1991Important for dimerization By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57BW7 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 65C4C1B754D13CE0

FASTA30335,111
        10         20         30         40         50         60 
MKREDIPAII PADIEEKKKA AQSWFEELRD RICASYEQLE DELQGPLSDR EPGRFVRTPW 

        70         80         90        100        110        120 
QKDDGNGGGV MSIMHGRVFE KVGVHVSTVH GEFSPEFRKQ IPGAEEDPRY WASGISLIAH 

       130        140        150        160        170        180 
PQNPNVPAVH MNTRMIVTTR QWFAGGADLT PVLDRRRTQE DPDTLAFHKA FRFICEKHKD 

       190        200        210        220        230        240 
IVDYQRLKEW CDEYFFLPHR DEPRGIGGIF YDWLHSPEEK GGWDSDFAFT RDVGRGFSVV 

       250        260        270        280        290        300 
YPHLVRQNFN KDWTEADRDE QLIRRGRYVE FNLLYDRGTI FGLKTGGNMN AILSSMPPVV 


KWP 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017223 Genomic DNA. Translation: AAX74867.1.
RefSeqYP_222228.1. NC_006932.1.

3D structure databases

HSSPHSSP built from PDB template 1TK1 based on UniProtKB P11353.
ProteinModelPortalQ57BW7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3341076.
GenomeReviewsGene locus BruAb1_1539 in contig AE017223_GR.
KEGGbmb:BruAb1_1539.
PATRIC17824828. VBIBruAbo15061_1628.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG631180.
OMAVKAYLLD.
PhylomeDBQ57BW7.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycBABO262698:BRUAB1_1539-MONOMER.

Family and domain databases

HAMAPMF_00333. Coprogen_oxidas.
[Tree]
InterProIPR001260. Coprogen_oxidase_aer.
IPR018375. Coprogen_oxidase_CS.
[Graphical view]
Gene3DG3DSA:3.40.1500.10. Coprogen_oxidas. 1 hit.
KOK00228.
PANTHERPTHR10755. Coprogen_oxidas. 1 hit.
PfamPF01218. Coprogen_oxidas. 1 hit.
[Graphical view]
PIRSFPIRSF000166. Coproporphyri_ox. 1 hit.
PRINTSPR00073. COPRGNOXDASE.
SUPFAMSSF102886. Coprogen_oxidas. 1 hit.
PROSITEPS01021. COPROGEN_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM6_BRUAB
AccessionPrimary (citable) accession number: Q57BW7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 10, 2005
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families