(data stored in SCRATCH zone)

SWISSPROT: C8U2G1_ECO10

ID   C8U2G1_ECO10            Unreviewed;       320 AA.
AC   C8U2G1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Ferrochelatase {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607};
DE            EC=4.99.1.1 {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607};
DE   AltName: Full=Heme synthase {ECO:0000256|HAMAP-Rule:MF_00323};
DE   AltName: Full=Protoheme ferro-lyase {ECO:0000256|HAMAP-Rule:MF_00323};
GN   Name=hemH {ECO:0000256|HAMAP-Rule:MF_00323,
GN   ECO:0000313|EMBL:BAI29319.1};
GN   OrderedLocusNames=ECO103_0451 {ECO:0000313|EMBL:BAI29319.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29319.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29319.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC       {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607,
CC       ECO:0000256|SAAS:SAAS00982002}.
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:0000256|HAMAP-Rule:MF_00323,
CC         ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS01116640};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607,
CC       ECO:0000256|SAAS:SAAS00710563}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00323}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00323}.
CC   -!- SIMILARITY: Belongs to the ferrochelatase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU004185,
CC       ECO:0000256|SAAS:SAAS00710585}.
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DR   EMBL; AP010958; BAI29319.1; -; Genomic_DNA.
DR   RefSeq; WP_001250096.1; NC_013353.1.
DR   EnsemblBacteria; BAI29319; BAI29319; ECO103_0451.
DR   KEGG; eoh:ECO103_0451; -.
DR   HOGENOM; HOG000060730; -.
DR   KO; K01772; -.
DR   OMA; LGDPYHC; -.
DR   BioCyc; ECOL585395:ECO103_RS02360-MONOMER; -.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; C8U2G1.
DR   SWISS-2DPAGE; C8U2G1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00323};
KW   Heme biosynthesis {ECO:0000256|HAMAP-Rule:MF_00323,
KW   ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS00710567};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607,
KW   ECO:0000256|SAAS:SAAS00710560};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607,
KW   ECO:0000256|SAAS:SAAS00710535};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00323,
KW   ECO:0000256|SAAS:SAAS00982033};
KW   Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00323,
KW   ECO:0000256|RuleBase:RU000607, ECO:0000256|SAAS:SAAS00710550}.
FT   METAL       194    194       Iron. {ECO:0000256|HAMAP-Rule:MF_00323}.
FT   METAL       275    275       Iron. {ECO:0000256|HAMAP-Rule:MF_00323}.
SQ   SEQUENCE   320 AA;  35912 MW;  F8838C4C0323F226 CRC64;
     MRQTKTGILL ANLGTPDAPT PEAVKRYLKQ FLSDRRVVDT SRLLWWPLLR GVILPLRSPR
     VAKLYASVWM EDGSPLMVYS RQQQQALAQR LPETPVALGM SYGSPSLESA VDELLAEHVD
     HIVVLPLYPQ FSCSTVGAVW DELARILARK RSIPGISFIR DYADNHDYIN ALANSVRASF
     AKHGEPDLLL LSYHGIPQRY ADEGDDYPQR CRTTTRELAS ALGMAPEKVM MTFQSRFGRE
     PWLMPYTDET LKMLGEKGVG HIQVMCPGFA ADCLETLEEI AEQNREVFLG AGGKKYEYIP
     ALNATPEHIE MMANLVAAYR
//

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