(data stored in ACNUC7421 zone)

SWISSPROT: HEMH_ECODH

ID   HEMH_ECODH              Reviewed;         320 AA.
AC   B1XFR2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 56.
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};
GN   OrderedLocusNames=ECDH10B_0431;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC       {ECO:0000255|HAMAP-Rule:MF_00323}.
CC   -!- CATALYTIC ACTIVITY: Protoheme + 2 H(+) = protoporphyrin + Fe(2+).
CC       {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   -!- SIMILARITY: Belongs to the ferrochelatase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00323}.
DR   EMBL; CP000948; ACB01602.1; -; Genomic_DNA.
DR   RefSeq; WP_001250103.1; NC_010473.1.
DR   ProteinModelPortal; B1XFR2; -.
DR   SMR; B1XFR2; -.
DR   EnsemblBacteria; ACB01602; ACB01602; ECDH10B_0431.
DR   KEGG; ecd:ECDH10B_0431; -.
DR   eggNOG; ENOG4105CFX; Bacteria.
DR   eggNOG; COG0276; LUCA.
DR   HOGENOM; HOG000060730; -.
DR   KO; K01772; -.
DR   OMA; LGDPYHC; -.
DR   UniPathway; UPA00252; UER00325.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
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; B1XFR2.
DR   SWISS-2DPAGE; B1XFR2.
KW   Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW   Porphyrin biosynthesis.
FT   CHAIN         1    320       Ferrochelatase.
FT                                /FTId=PRO_1000116043.
FT   METAL       194    194       Iron. {ECO:0000255|HAMAP-Rule:MF_00323}.
FT   METAL       275    275       Iron. {ECO:0000255|HAMAP-Rule:MF_00323}.
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
//

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