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P32396 (HEMH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
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
Synonyms:hemF
Ordered Locus Names:BSU10130
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the ferrous insertion into protoporphyrin IX. HAMAP-Rule MF_00323

Catalytic activity

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

Pathway

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

Subcellular location

Cytoplasm HAMAP-Rule MF_00323.

Sequence similarities

Belongs to the ferrochelatase family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheme biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionferrochelatase activity

Inferred from electronic annotation. Source: HAMAP

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 – 310310Ferrochelatase HAMAP-Rule MF_00323
PRO_0000175114

Sites

Metal binding1831Iron
Metal binding2641Iron

Secondary structure

1 .................................................. 310
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32396 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 5BFD9972689CE761

FASTA31035,348
        10         20         30         40         50         60 
MSRKKMGLLV MAYGTPYKEE DIERYYTHIR RGRKPEPEML QDLKDRYEAI GGISPLAQIT 

        70         80         90        100        110        120 
EQQAHNLEQH LNEIQDEITF KAYIGLKHIE PFIEDAVAEM HKDGITEAVS IVLAPHFSTF 

       130        140        150        160        170        180 
SVQSYNKRAK EEAEKLGGLT ITSVESWYDE PKFVTYWVDR VKETYASMPE DERENAMLIV 

       190        200        210        220        230        240 
SAHSLPEKIK EFGDPYPDQL HESAKLIAEG AGVSEYAVGW QSEGNTPDPW LGPDVQDLTR 

       250        260        270        280        290        300 
DLFEQKGYQA FVYVPVGFVA DHLEVLYDND YECKVVTDDI GASYYRPEMP NAKPEFIDAL 

       310 
ATVVLKKLGR

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes."
Hansson M., Hederstedt L.
J. Bacteriol. 174:8081-8093(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis."
Al-Karadaghi S., Hansson M., Nikonov S., Jonsson B., Hederstedt L.
Structure 5:1501-1510(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[5]"Structural and mechanistic basis of porphyrin metallation by ferrochelatase."
Lecerof D., Fodje M., Hansson A., Hansson M., Al-Karadaghi S.
J. Mol. Biol. 297:221-232(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[6]"Structure prediction and fold recognition for the ferrochelatase family of proteins."
Hansson M., Gough S.P., Brody S.S.
Proteins 27:517-522(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M97208 Genomic DNA. Translation: AAA22518.1.
Y14083 Genomic DNA. Translation: CAA74519.1.
AL009126 Genomic DNA. Translation: CAB12853.1.
PIRC47045.
RefSeqNP_388894.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AK1X-ray1.90A1-310[»]
1C1HX-ray1.90A1-310[»]
1C9EX-ray2.30A5-310[»]
1DOZX-ray1.80A2-310[»]
1FJImodel-A1-310[»]
1LD3X-ray2.60A1-310[»]
1N0IX-ray2.00A1-310[»]
2AC2X-ray2.50A2-310[»]
2AC4X-ray2.10A2-310[»]
2H1VX-ray1.20A1-310[»]
2H1WX-ray2.60A1-310[»]
2HK6X-ray1.71A1-310[»]
2Q2NX-ray1.80A2-310[»]
2Q2OX-ray2.10A2-310[»]
2Q3JX-ray2.39A2-310[»]
3GOQX-ray1.60A1-310[»]
3M4ZX-ray1.94A2-310[»]
ProteinModelPortalP32396.
SMRP32396. Positions 2-310.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU10130.

Proteomic databases

PaxDbP32396.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12853; CAB12853; BSU10130.
GeneID939772.
KEGGbsu:BSU10130.
PATRIC18973724. VBIBacSub10457_1056.

Organism-specific databases

GenoListBSU10130. [Micado]

Phylogenomic databases

eggNOGCOG0276.
HOGENOMHOG000060729.
KOK01772.
OMAWNNSSEV.
ProtClustDBPRK12435.

Enzyme and pathway databases

BioCycBSUB:BSU10130-MONOMER.
BRENDA4.99.1.1. 700.
UniPathwayUPA00252; UER00325.

Family and domain databases

HAMAPMF_00323. Ferrochelatase.
InterProIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
PANTHERPTHR11108. PTHR11108. 1 hit.
PfamPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00109. hemH. 1 hit.
PROSITEPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32396.

Entry information

Entry nameHEMH_BACSU
AccessionPrimary (citable) accession number: P32396
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 29, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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