HEMH_ECOLI
ID HEMH_ECOLI Reviewed; 320 AA.
AC P23871; P78232; Q2MBV2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323};
DE EC=4.99.1.1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Heme synthase {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Protoheme ferro-lyase {ECO:0000255|HAMAP-Rule:MF_00323};
GN Name=hemH {ECO:0000255|HAMAP-Rule:MF_00323}; Synonyms=popA, visA;
GN OrderedLocusNames=b0475, JW0464;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=2051480; DOI=10.1016/0022-2836(91)90180-e;
RA Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.;
RT "Isolation and characterization of visible light-sensitive mutants of
RT Escherichia coli K12.";
RL J. Mol. Biol. 219:393-398(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RX PubMed=8056770; DOI=10.1093/oxfordjournals.jbchem.a124373;
RA Miyamoto K., Kanaya S., Morikawa K., Inokuchi H.;
RT "Overproduction, purification, and characterization of ferrochelatase from
RT Escherichia coli.";
RL J. Biochem. 115:545-551(1994).
RN [3]
RP SEQUENCE REVISION TO 54.
RA Miyamoto K.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8458858; DOI=10.1128/jb.175.7.2154-2156.1993;
RA Frustaci J.M., O'Brian M.R.;
RT "The Escherichia coli visA gene encodes ferrochelatase, the final enzyme of
RT the heme biosynthetic pathway.";
RL J. Bacteriol. 175:2154-2156(1993).
CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX;
CC Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00323};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- DISRUPTION PHENOTYPE: Cells are sensitive to visible light (which is
CC lethal). {ECO:0000269|PubMed:2051480}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000255|HAMAP-
CC Rule:MF_00323, ECO:0000305}.
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DR EMBL; D90259; BAA14304.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40229.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73577.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76254.1; -; Genomic_DNA.
DR PIR; B64778; B64778.
DR RefSeq; NP_415008.1; NC_000913.3.
DR RefSeq; WP_001250103.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P23871; -.
DR SMR; P23871; -.
DR BioGRID; 4259849; 7.
DR BioGRID; 851849; 1.
DR IntAct; P23871; 9.
DR STRING; 511145.b0475; -.
DR jPOST; P23871; -.
DR PaxDb; P23871; -.
DR PRIDE; P23871; -.
DR EnsemblBacteria; AAC73577; AAC73577; b0475.
DR EnsemblBacteria; BAE76254; BAE76254; BAE76254.
DR GeneID; 947532; -.
DR KEGG; ecj:JW0464; -.
DR KEGG; eco:b0475; -.
DR PATRIC; fig|1411691.4.peg.1801; -.
DR EchoBASE; EB0426; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_0_0_6; -.
DR InParanoid; P23871; -.
DR OMA; LGDPYHC; -.
DR PhylomeDB; P23871; -.
DR BioCyc; EcoCyc:PROTOHEME-FERROCHELAT-MON; -.
DR BioCyc; MetaCyc:PROTOHEME-FERROCHELAT-MON; -.
DR UniPathway; UPA00252; UER00325.
DR PRO; PR:P23871; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IDA:EcoliWiki.
DR GO; GO:0046501; P:protoporphyrinogen IX metabolic process; IMP:EcoliWiki.
DR GO; GO:0009416; P:response to light stimulus; IMP:EcoliWiki.
DR CDD; cd00419; Ferrochelatase_C; 1.
DR CDD; cd03411; Ferrochelatase_N; 1.
DR HAMAP; MF_00323; Ferrochelatase; 1.
DR InterPro; IPR001015; Ferrochelatase.
DR InterPro; IPR019772; Ferrochelatase_AS.
DR InterPro; IPR033644; Ferrochelatase_C.
DR InterPro; IPR033659; Ferrochelatase_N.
DR PANTHER; PTHR11108; PTHR11108; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
DR TIGRFAMs; TIGR00109; hemH; 1.
DR PROSITE; PS00534; FERROCHELATASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Heme biosynthesis; Iron; Lyase;
KW Metal-binding; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..320
FT /note="Ferrochelatase"
FT /id="PRO_0000175138"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT CONFLICT 54
FT /note="L -> F (in Ref. 1; BAA14304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35884 MW; 65BB56EBFDD95D5C CRC64;
MRQTKTGILL ANLGTPDAPT PEAVKRYLKQ FLSDRRVVDT SRLLWWPLLR GVILPLRSPR
VAKLYASVWM EGGSPLMVYS RQQQQALAQR LPEMPVALGM SYGSPSLESA VDELLAEHVD
HIVVLPLYPQ FSCSTVGAVW DELARILARK RSIPGISFIR DYADNHDYIN ALANSVRASF
AKHGEPDLLL LSYHGIPQRY ADEGDDYPQR CRTTTRELAS ALGMAPEKVM MTFQSRFGRE
PWLMPYTDET LKMLGEKGVG HIQVMCPGFA ADCLETLEEI AEQNREVFLG AGGKKYEYIP
ALNATPEHIE MMANLVAAYR
