Skip Header

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

O04921 (HEMH2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferrochelatase-2, chloroplastic
EC=4.99.1.1
Alternative name(s):
Ferrochelatase II
Heme synthase 2
Protoheme ferro-lyase 2
Gene names
Ordered Locus Names:At2g30390
ORF Names:T06B20.24, T9D9.1
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

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

Plastid › chloroplast membrane; Peripheral membrane protein. Plastid › chloroplast thylakoid membrane; Peripheral membrane protein Ref.5.

Sequence similarities

Belongs to the ferrochelatase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionferrochelatase activity

Inferred from genetic interaction Ref.1. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: O04921-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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
Isoform 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]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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.
[5]"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.
AC002338 Genomic DNA. Translation: AAM14820.1.
U93215 Genomic DNA. Translation: AAB63095.1.
CP002685 Genomic DNA. Translation: AEC08379.1.
BT000465 mRNA. Translation: AAN17442.1.
BT008877 mRNA. Translation: AAP68316.1.
IPIIPI00534550.
PIRH84707.
RefSeqNP_180598.1. NM_128592.2.
UniGeneAt.22966.

3D structure databases

ProteinModelPortalO04921.
SMRO04921. Positions 97-426, 473-503.
ModBaseSearch...

Protein-protein interaction databases

IntActO04921. 4 interactions.
STRINGO04921.

Proteomic databases

PRIDEO04921.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G30390.1; AT2G30390.1; AT2G30390.
GeneID817589.
GenomeReviewsGene locus AT2G30390 in contig CT485783_GR.
KEGGath:AT2G30390.
NMPDRfig|3702.1.peg.10090.

Organism-specific databases

TAIRAt2g30390.

Phylogenomic databases

eggNOGKOG1321.
GeneTreeEPGT00050000010201.
HOGENOMHBG697135.
InParanoidO04921.
OMALQKPLAW.
PhylomeDBO04921.
ProtClustDBPLN02449.

Enzyme and pathway databases

BioCycARA:AT2G30390-MONOMER.

Gene expression databases

ArrayExpressO04921.
GenevestigatorO04921.
GermOnlineAT2G30390. Arabidopsis thaliana.

Family and domain databases

InterProIPR022796. Chloroa_b-bind.
IPR023329. Chlorophyll_a/b-bd_dom.
IPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
Gene3DG3DSA:1.10.3460.10. G3DSA:1.10.3460.10. 1 hit.
KOK01772.
PANTHERPTHR11108. Ferrochelatase. 1 hit.
PfamPF00504. Chloroa_b-bind. 1 hit.
PF00762. Ferrochelatase. 1 hit.
[Graphical view]
SUPFAMSSF103511. SSF103511. 1 hit.
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: December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents