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Protein

Ferrochelatase

Gene

hemH

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ferrous insertion into protoporphyrin IX.

Catalytic activityi

Protoheme + 2 H+ = protoporphyrin + Fe2+.

Pathwayi: protoheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes protoheme from protoporphyrin-IX.
Proteins known to be involved in this subpathway in this organism are:
  1. Ferrochelatase (hemH)
This subpathway is part of the pathway protoheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protoheme from protoporphyrin-IX, the pathway protoheme biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi183 – 1831Iron
Metal bindingi264 – 2641Iron

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU10130-MONOMER.
BRENDAi4.99.1.1. 658.
UniPathwayiUPA00252; UER00325.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferrochelatase (EC:4.99.1.1)
Alternative name(s):
Heme synthase
Protoheme ferro-lyase
Gene namesi
Name:hemH
Synonyms:hemF
Ordered Locus Names:BSU10130
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310FerrochelatasePRO_0000175114Add
BLAST

Proteomic databases

PaxDbiP32396.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005631.

Structurei

Secondary structure

1
310
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Helixi19 – 213Combined sources
Helixi22 – 298Combined sources
Turni30 – 323Combined sources
Helixi37 – 4913Combined sources
Helixi54 – 7421Combined sources
Beta strandi76 – 9217Combined sources
Helixi93 – 10210Combined sources
Beta strandi107 – 11610Combined sources
Turni119 – 1213Combined sources
Helixi122 – 13615Combined sources
Beta strandi140 – 1434Combined sources
Helixi151 – 16717Combined sources
Helixi170 – 1734Combined sources
Beta strandi175 – 1839Combined sources
Helixi187 – 1926Combined sources
Helixi196 – 21116Combined sources
Beta strandi216 – 2227Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi230 – 2323Combined sources
Helixi235 – 24612Combined sources
Beta strandi249 – 2546Combined sources
Beta strandi260 – 2623Combined sources
Helixi263 – 2664Combined sources
Turni267 – 2715Combined sources
Helixi272 – 2809Combined sources
Beta strandi283 – 2853Combined sources
Helixi294 – 30714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP32396.
SMRiP32396. Positions 2-310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32396.

Family & Domainsi

Sequence similaritiesi

Belongs to the ferrochelatase family.Curated

Phylogenomic databases

eggNOGiENOG4107TTW. Bacteria.
COG0276. LUCA.
HOGENOMiHOG000060729.
InParanoidiP32396.
KOiK01772.
OMAiMHKDGIT.
OrthoDBiEOG6XHC5H.
PhylomeDBiP32396.

Family and domain databases

HAMAPiMF_00323. Ferrochelatase.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
PANTHERiPTHR11108. PTHR11108. 1 hit.
PfamiPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00109. hemH. 1 hit.
PROSITEiPS00534. FERROCHELATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRKKMGLLV MAYGTPYKEE DIERYYTHIR RGRKPEPEML QDLKDRYEAI
60 70 80 90 100
GGISPLAQIT EQQAHNLEQH LNEIQDEITF KAYIGLKHIE PFIEDAVAEM
110 120 130 140 150
HKDGITEAVS IVLAPHFSTF SVQSYNKRAK EEAEKLGGLT ITSVESWYDE
160 170 180 190 200
PKFVTYWVDR VKETYASMPE DERENAMLIV SAHSLPEKIK EFGDPYPDQL
210 220 230 240 250
HESAKLIAEG AGVSEYAVGW QSEGNTPDPW LGPDVQDLTR DLFEQKGYQA
260 270 280 290 300
FVYVPVGFVA DHLEVLYDND YECKVVTDDI GASYYRPEMP NAKPEFIDAL
310
ATVVLKKLGR
Length:310
Mass (Da):35,348
Last modified:October 1, 1993 - v1
Checksum:i5BFD9972689CE761
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97208 Genomic DNA. Translation: AAA22518.1.
Y14083 Genomic DNA. Translation: CAA74519.1.
AL009126 Genomic DNA. Translation: CAB12853.1.
PIRiC47045.
RefSeqiNP_388894.1. NC_000964.3.
WP_003244736.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB12853; CAB12853; BSU10130.
GeneIDi939772.
KEGGibsu:BSU10130.
PATRICi18973724. VBIBacSub10457_1056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97208 Genomic DNA. Translation: AAA22518.1.
Y14083 Genomic DNA. Translation: CAA74519.1.
AL009126 Genomic DNA. Translation: CAB12853.1.
PIRiC47045.
RefSeqiNP_388894.1. NC_000964.3.
WP_003244736.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP32396.
SMRiP32396. Positions 2-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005631.

Proteomic databases

PaxDbiP32396.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12853; CAB12853; BSU10130.
GeneIDi939772.
KEGGibsu:BSU10130.
PATRICi18973724. VBIBacSub10457_1056.

Phylogenomic databases

eggNOGiENOG4107TTW. Bacteria.
COG0276. LUCA.
HOGENOMiHOG000060729.
InParanoidiP32396.
KOiK01772.
OMAiMHKDGIT.
OrthoDBiEOG6XHC5H.
PhylomeDBiP32396.

Enzyme and pathway databases

UniPathwayiUPA00252; UER00325.
BioCyciBSUB:BSU10130-MONOMER.
BRENDAi4.99.1.1. 658.

Miscellaneous databases

EvolutionaryTraceiP32396.

Family and domain databases

HAMAPiMF_00323. Ferrochelatase.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
PANTHERiPTHR11108. PTHR11108. 1 hit.
PfamiPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00109. hemH. 1 hit.
PROSITEiPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiHEMH_BACSU
AccessioniPrimary (citable) accession number: P32396
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: February 17, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.