P23871 (HEMH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferrochelatase
EC=4.99.1.1

Alternative name(s):
Heme synthase
Protoheme ferro-lyase

Gene names

Name:	hemH
Synonyms:	popA, visA
Ordered Locus Names:	b0475, JW0464

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Protein existence	Evidence 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 metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. HAMAP-Rule MF_00323
Subunit structure	Monomer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00323.
Disruption phenotype	Cells are sensitive to visible light (which is lethal). Ref.1
Sequence similarities	Belongs to the ferrochelatase family.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	heme biosynthetic process Inferred from direct assay Ref.7. Source: EcoliWiki protoporphyrinogen IX metabolic process Inferred from mutant phenotype PubMed 1397280. Source: EcoliWiki response to light stimulus Inferred from mutant phenotype PubMed 1835790Ref.1. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ferrochelatase activity Inferred from direct assay Ref.2. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 320	320	Ferrochelatase HAMAP-Rule MF_00323		PRO_0000175138
Sites
	Metal binding	194	1	Iron By similarity
	Metal binding	275	1	Iron By similarity
Experimental info
	Sequence conflict	54	1	L → F in BAA14304. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23871 [UniParc]. Last modified November 1, 1997. Version 3. Checksum: 65BB56EBFDD95D5C	FASTA	320	35,884
	10 20 30 40 50 60 MRQTKTGILL ANLGTPDAPT PEAVKRYLKQ FLSDRRVVDT SRLLWWPLLR GVILPLRSPR 70 80 90 100 110 120 VAKLYASVWM EGGSPLMVYS RQQQQALAQR LPEMPVALGM SYGSPSLESA VDELLAEHVD 130 140 150 160 170 180 HIVVLPLYPQ FSCSTVGAVW DELARILARK RSIPGISFIR DYADNHDYIN ALANSVRASF 190 200 210 220 230 240 AKHGEPDLLL LSYHGIPQRY ADEGDDYPQR CRTTTRELAS ALGMAPEKVM MTFQSRFGRE 250 260 270 280 290 300 PWLMPYTDET LKMLGEKGVG HIQVMCPGFA ADCLETLEEI AEQNREVFLG AGGKKYEYIP 310 320 ALNATPEHIE MMANLVAAYR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12." Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H. J. Mol. Biol. 219:393-398(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE. Strain: K12.
[2]	"Overproduction, purification, and characterization of ferrochelatase from Escherichia coli." Miyamoto K., Kanaya S., Morikawa K., Inokuchi H. J. Biochem. 115:545-551(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
[3]	Miyamoto K. Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 54.
[4]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"The Escherichia coli visA gene encodes ferrochelatase, the final enzyme of the heme biosynthetic pathway." Frustaci J.M., O'Brian M.R. J. Bacteriol. 175:2154-2156(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D90259 Genomic DNA. Translation: BAA14304.1. U82664 Genomic DNA. Translation: AAB40229.1. U00096 Genomic DNA. Translation: AAC73577.1. AP009048 Genomic DNA. Translation: BAE76254.1.
PIR	B64778.
RefSeq	NP_415008.1. NC_000913.2. YP_488766.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P23871.
SMR	P23871. Positions 6-319.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23871. 8 interactions.
STRING	511145.b0475.
Proteomic databases
PaxDb	P23871.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73577; AAC73577; b0475. BAE76254; BAE76254; BAE76254.
GeneID	12930855. 947532.
KEGG	ecj:Y75_p0462. eco:b0475.
PATRIC	32116107. VBIEscCol129921_0495.
Organism-specific databases
EchoBASE	EB0426.
EcoGene	EG10431. hemH.
Phylogenomic databases
eggNOG	COG0276.
HOGENOM	HOG000060730.
KO	K01772.
OMA	TLYELDM.
ProtClustDB	PRK00035.
Enzyme and pathway databases
BioCyc	EcoCyc:PROTOHEME-FERROCHELAT-MONOMER. ECOL316407:JW0464-MONOMER. MetaCyc:PROTOHEME-FERROCHELAT-MONOMER.
UniPathway	UPA00252; UER00325.
Gene expression databases
Genevestigator	P23871.
Family and domain databases
HAMAP	MF_00323. Ferrochelatase.
InterPro	IPR001015. Ferrochelatase. IPR019772. Ferrochelatase_AS. [Graphical view]
PANTHER	PTHR11108. PTHR11108. 1 hit.
Pfam	PF00762. Ferrochelatase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00109. hemH. 1 hit.
PROSITE	PS00534. FERROCHELATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEMH_ECOLI

Accession

Primary (citable) accession number: P23871
Secondary accession number(s): P78232, Q2MBV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program