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Reviewed, UniProtKB/Swiss-Prot O04921 (HEMH2_ARATH)

Last modified February 9, 2010. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ferrochelatase-2, chloroplastic
    EC=4.99.1.1
Alternative name(s):
    Ferrochelatase II
    Protoheme ferro-lyase 2
    Heme synthetase 2
Gene names
Ordered Locus Names: At2g30390
ORF Names: T06B20.24, T9D9.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the ferrous insertion into protoporphyrin IX. May have a role in dealing with oxidative stress.

Catalytic activity

Protoheme + 2 H+ = protoporphyrin + Fe2+.

Pathway

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

Subcellular location

Plastidchloroplast membrane; Peripheral membrane protein. Plastidchloroplast thylakoid membrane; Peripheral membrane protein Ref.4.

Sequence similarities

Belongs to the ferrochelatase family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   DomainTransit peptide
   LigandIron
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processheme biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

photosynthesis, light harvesting

Inferred from electronic annotation. Source: InterPro

   Cellular componentchloroplast Ref.1

Inferred from direct assay. Source: TAIR

extrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

thylakoid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionferrochelatase activity Ref.1

Inferred from genetic interaction. Source: TAIR

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 512Ferrochelatase-2, chloroplasticPRO_0000008881

Regions

Compositional bias9 – 1911Poly-Ser
Compositional bias23 – 264Poly-Pro
Compositional bias80 – 834Poly-Ser
Compositional bias90 – 934Poly-Ser

Experimental info

Sequence conflict156 – 1594SKEG → ARR in CAA73614. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O04921-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 521B1FC596E844A7

FASTA51256,619
        10         20         30         40         50         60 
MNCPAMTASP SSSSSSSYST FRPPPPLLPQ LSNDSQRSVV MHCTRLPFEA FAATSSNRLL 

        70         80         90        100        110        120 
GKHSLPLRAA LVTSNPLNIS SSSVISDAIS SSSVITDDAK IGVLLLNLGG PETLDDVQPF 

       130        140        150        160        170        180 
LFNLFADPDI IRLPPVFQFL QKPLAQFISV ARAPKSKEGY ASIGGGSPLR HITDAQAEEL 

       190        200        210        220        230        240 
RKCLWEKNVP AKVYVGMRYW HPFTEEAIEQ IKRDGITKLV VLPLYPQFSI STSGSSLRLL 

       250        260        270        280        290        300 
ERIFREDEYL VNMQHTVIPS WYQREGYIKA MANLIQSELG KFGSPNQVVI FFSAHGVPLA 

       310        320        330        340        350        360 
YVEEAGDPYK AEMEECVDLI MEELDKRKIT NAYTLAYQSR VGPVEWLKPY TEEAITELGK 

       370        380        390        400        410        420 
KGVENLLAVP ISFVSEHIET LEEIDVEYKE LALKSGIKNW GRVPALGTEP MFISDLADAV 

       430        440        450        460        470        480 
VESLPYVGAM AVSNLEARQS LVPLGSVEEL LATYDSQRRE LPAPVTMWEW GWTKSAETWN 

       490        500        510 
GRAAMLAVLA LLVLEVTTGK GFLHQWGILP SL 

« Hide

References

« Hide 'large scale' references
[1]"Two different genes encode ferrochelatase in Arabidopsis: mapping, expression and subcellular targeting of the precursor proteins."
Chow K.-S., Singh D.P., Walker A., Smith A.G.
Plant J. 15:531-541(1998) [PubMed: 9753778] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
Tissue: Seedling.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Molecular localisation of ferrochelatase in higher plant chloroplasts."
Roper J.M., Smith A.G.
Eur. J. Biochem. 246:32-37(1997) [PubMed: 9210462] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13156 mRNA. Translation: CAA73614.1.
U93215 Genomic DNA. Translation: AAB63095.1.
AC002338 Genomic DNA. Translation: AAM14820.1.
BT000465 mRNA. Translation: AAN17442.1.
BT008877 mRNA. Translation: AAP68316.1.
IPIIPI00534550.
PIRH84707.
RefSeqNP_180598.1.
UniGeneAt.22966
Rsa.2561

3D structure databases

SMRO04921. Positions 99-425.
ModBaseSearch...

Protein-protein interaction databases

STRINGO04921.

Proteomic databases

PRIDEO04921.

Genome annotation databases

GeneID817589.
GenomeReviewsGene locus AT2G30390 in contig CT485783_GR.
KEGGath:AT2G30390.
NMPDRfig|3702.1.peg.10090.

Organism-specific databases

TAIRAt2g30390.

Phylogenomic databases

eggNOGKOG1321.
HOGENOMHBG697135.
InParanoidO04921.
OMAWLQKPLA.
PhylomeDBO04921.

Enzyme and pathway databases

BRENDA4.99.1.1. 302.

Gene expression databases

ArrayExpressO04921.
GenevestigatorO04921.
GermOnlineAT2G30390. Arabidopsis thaliana.

Family and domain databases

InterProIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
PANTHERPTHR11108. Ferrochelatase. 1 hit.
PfamPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00109. hemH. 1 hit.
PROSITEPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEMH2_ARATH
AccessionPrimary (citable) accession number: O04921
Secondary accession number(s): O23623, Q7GB39
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: February 9, 2010
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents