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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)DescriptionActionsGraphical viewLength
Metal bindingi183Iron1
Metal bindingi264Iron1

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.
MetaCyc: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)DescriptionActionsGraphical viewLength
ChainiPRO_00001751141 – 310FerrochelataseAdd BLAST310

Proteomic databases

PaxDbiP32396.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005631.

Structurei

Secondary structure

1310
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Helixi19 – 21Combined sources3
Helixi22 – 29Combined sources8
Turni30 – 32Combined sources3
Helixi37 – 49Combined sources13
Helixi54 – 74Combined sources21
Beta strandi76 – 92Combined sources17
Helixi93 – 102Combined sources10
Beta strandi107 – 116Combined sources10
Turni119 – 121Combined sources3
Helixi122 – 136Combined sources15
Beta strandi140 – 143Combined sources4
Helixi151 – 167Combined sources17
Helixi170 – 173Combined sources4
Beta strandi175 – 183Combined sources9
Helixi187 – 192Combined sources6
Helixi196 – 211Combined sources16
Beta strandi216 – 222Combined sources7
Beta strandi226 – 228Combined sources3
Beta strandi230 – 232Combined sources3
Helixi235 – 246Combined sources12
Beta strandi249 – 254Combined sources6
Beta strandi260 – 262Combined sources3
Helixi263 – 266Combined sources4
Turni267 – 271Combined sources5
Helixi272 – 280Combined sources9
Beta strandi283 – 285Combined sources3
Helixi294 – 307Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
PhylomeDBiP32396.

Family and domain databases

CDDicd00419. Ferrochelatase_C. 1 hit.
cd03411. Ferrochelatase_N. 1 hit.
HAMAPiMF_00323. Ferrochelatase. 1 hit.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
IPR033644. Ferrochelatase_C.
IPR033659. Ferrochelatase_N.
[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
PDB 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.
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.
PhylomeDBiP32396.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP32396.

Family and domain databases

CDDicd00419. Ferrochelatase_C. 1 hit.
cd03411. Ferrochelatase_N. 1 hit.
HAMAPiMF_00323. Ferrochelatase. 1 hit.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
IPR033644. Ferrochelatase_C.
IPR033659. Ferrochelatase_N.
[Graphical view]
PANTHERiPTHR11108. PTHR11108. 1 hit.
PfamiPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00109. hemH. 1 hit.
PROSITEiPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 132 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.