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Q7V2F5 (HEMH_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Ferrochelatase

EC=4.99.1.1
Alternative name(s):
Heme synthase
Protoheme ferro-lyase
Gene names
Name:hemH
Ordered Locus Names:PMM0525
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the ferrous insertion into protoporphyrin IX. 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
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 – 391391Ferrochelatase HAMAP MF_00323
PRO_0000175182

Sites

Metal binding1961Iron By similarity
Metal binding2811Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V2F5 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 01633FB50CB48414

FASTA39144,195
        10         20         30         40         50         60 
MEKVGVLLMN LGGPERITDV GPFLYNLFSD PEIIRLPVPA FQKPLAWLIS TLRSTTSQQA 

        70         80         90        100        110        120 
YLSIGGGSPI RRITEQQARE LQSKLRDKGL NVTTYIAMRY WHPFTESAIA DMKADGVDQI 

       130        140        150        160        170        180 
VVLPLYPHFS ISTSGSSFRE LKKLRDSDSE FQKIPMRCVR SWFSQSGYLK SMVELISEQI 

       190        200        210        220        230        240 
SLCESPDSAH IFFTAHGVPK SYVEEAGDPY KEQIEDCSLL IIDELEKYLG HTNPYTLSYQ 

       250        260        270        280        290        300 
SRVGPVEWLK PYTEEVLTDL GKAKVNDLIV VPISFVGEHI ETLQEIDIEY KEIAEKAGIV 

       310        320        330        340        350        360 
NFRRVKALNT HPTFIDGLSE LVVSCLEGPI INIEKASELP EKVKLYPQEK WQWGWNNSSE 

       370        380        390 
VWNGRVAMIV FLILFIELIS GSGPLHKLGI L 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE18984.1.
RefSeqNP_892643.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V2F5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7V2F5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1726744.
GenomeReviewsGene locus PMM0525 in contig BX548174_GR.
KEGGpmm:PMM0525.
NMPDRfig|59919.1.peg.522.
PATRIC23031820. VBIProMar68066_0580.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0276.
HOGENOMHBG697135.
OMALQKPLAW.
PhylomeDBQ7V2F5.
ProtClustDBPRK00035.

Enzyme and pathway databases

BioCycPMAR167540:PMM0525-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_PROMP
AccessionPrimary (citable) accession number: Q7V2F5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 56 of the entry and version 1 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