(data stored in ACNUC29543 zone)

SWISSPROT: HEMH_ACIBT

ID   HEMH_ACIBT              Reviewed;         338 AA.
AC   A3M1P7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, entry version 70.
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=A1S_0382;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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   -!- 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; CP000521; ABO10841.2; -; Genomic_DNA.
DR   EnsemblBacteria; ABO10841; ABO10841; A1S_0382.
DR   KEGG; acb:A1S_0382; -.
DR   HOGENOM; HOG000060730; -.
DR   KO; K01772; -.
DR   UniPathway; UPA00252; UER00325.
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; A3M1P7.
DR   SWISS-2DPAGE; A3M1P7.
KW   Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW   Porphyrin biosynthesis.
FT   CHAIN         1    338       Ferrochelatase.
FT                                /FTId=PRO_1000116024.
FT   METAL       202    202       Iron. {ECO:0000255|HAMAP-Rule:MF_00323}.
FT   METAL       283    283       Iron. {ECO:0000255|HAMAP-Rule:MF_00323}.
SQ   SEQUENCE   338 AA;  38269 MW;  A56E971106C298EA CRC64;
     MSFEQKPKVT VILANLGTPD EATVPAVRRF LKQFLSDPRV IEIPKFIWWI ILNLFVLPFR
     PKRVAHAYAS VWSTDSPMRE IVFEQTQRVQ AYLERENKQF DLTVLPAMTY GNPGIDAVLE
     KLSAHPQEHV ILLPLFPQYS ATSTAPLYDA FAKWIPTQRN LPGLTIIKDY YQHPMFIQAL
     AESVLAYQEQ HGKPEKLLMS FHGIPQPYAD KGDPYADRCR ITAKLVAEAL HLKDVEWAIS
     FQSRFGKQEW VKPYTDQLLQ DWAKQGVKSV QVLSPAFSAD CLETLEELAI QNAELFQQAG
     GGSYAYIPAL NSDQAHIDLL AGLVQANLDA LTHTLAHR
//

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