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P28602 (HEMH_BRAJA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ferrochelatase

EC=4.99.1.1
Alternative name(s):
Heme synthase
Protoheme ferro-lyase
Gene names
Name:hemH
Ordered Locus Names:bll7752
OrganismBradyrhizobium japonicum
Taxonomic identifier375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the ferrous insertion into protoporphyrin IX. Essential for normal nodule development. HAMAP MF_00323

Catalytic activity

Protoheme + 2 H+ = protoporphyrin + Fe2+. HAMAP MF_00323

Pathway

Porphyrin metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. HAMAP MF_00323

Subcellular location

Cytoplasm By similarity HAMAP MF_00323.

Sequence similarities

Belongs to the ferrochelatase family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processheme biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionferrochelatase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Ferrochelatase HAMAP MF_00323
PRO_0000175119

Sites

Metal binding2151Iron By similarity
Metal binding2961Iron By similarity

Experimental info

Sequence conflict151Q → R in AAA26217. Ref.1
Sequence conflict751T → S in AAA26217. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28602 [UniParc].

Last modified February 28, 2003. Version 3.
Checksum: 67833BFE08E0784C

FASTA34538,418
        10         20         30         40         50         60 
MSTAAPNETT QPTVQSGQKR VGVLLVNLGT PDTADAPGVR VYLKEFLSDA RVIEDQGLVW 

        70         80         90        100        110        120 
KVVLNGIILR SRPRTKALDY QKIWNNEKNE SPLKTITRSQ SDKLAAALSD RDHVVVDWAM 

       130        140        150        160        170        180 
RYGNPSIKSG IDALIAEGCD RILAVPLYPQ YSASTSATVC DEVFRVLARL RAQPTLRVTP 

       190        200        210        220        230        240 
PYYEDEAYIE ALAVSIETHL ATLPFKPELI VASFHGMPKS YVDKGDPYQE HCIATTEALR 

       250        260        270        280        290        300 
RRLGVDASKL LLTFQSRFGN DEWLQPYTDK TMERLAKEGV RRIAVVTPGF AADCLETLEE 

       310        320        330        340 
IAQENAEIFK HNGGEQFSAI PCLNDSEPGM DVIRTLVLRE LQGWI 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a Bradyrhizobium japonicum ferrochelatase mutant and isolation of the hemH gene."
Frustaci J.M., O'Brian M.R.
J. Bacteriol. 174:4223-4229(1992) [PubMed: 1624416] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LO.
[2]O'Brian M.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M92427 Genomic DNA. Translation: AAA26217.2.
BA000040 Genomic DNA. Translation: BAC53017.1.
PIRA42883.
RefSeqNP_774392.1. NC_004463.1.

3D structure databases

ProteinModelPortalP28602.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1047995.
GenomeReviewsGene locus bll7752 in contig BA000040_GR.
KEGGbja:bll7752.
NMPDRfig|224911.1.peg.7752.
PATRIC21199492. VBIBraJap65052_7974.

Phylogenomic databases

HOGENOMHBG697135.
OMATIEEIGM.
PhylomeDBP28602.
ProtClustDBPRK00035.

Enzyme and pathway databases

BioCycBJAP224911:BLL7752-MONOMER.

Family and domain databases

HAMAPMF_00323. Ferrochelatase.
[Tree]
InterProIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
KOK01772.
PANTHERPTHR11108. Ferrochelatase. 1 hit.
PfamPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00109. HemH. 1 hit.
PROSITEPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEMH_BRAJA
AccessionPrimary (citable) accession number: P28602
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 28, 2003
Last modified: January 25, 2012
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families