ID   HEMH_ANAVT              Reviewed;         388 AA.
AC   Q3MCT9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Ferrochelatase;
DE            EC=4.99.1.1;
DE   AltName: Full=Protoheme ferro-lyase;
DE   AltName: Full=Heme synthetase;
GN   Name=hemH; OrderedLocusNames=Ava_1574;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC   -!- CATALYTIC ACTIVITY: Protoheme + 2 H(+) = protoporphyrin + Fe(2+).
CC   -!- PATHWAY: Porphyrin metabolism; protoheme biosynthesis; protoheme
CC       from protoporphyrin-IX: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ferrochelatase family.
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DR   EMBL; CP000117; ABA21197.1; -; Genomic_DNA.
DR   RefSeq; YP_322092.1; -.
DR   GeneID; 3681117; -.
DR   GenomeReviews; CP000117_GR; Ava_1574.
DR   KEGG; ava:Ava_1574; -.
DR   NMPDR; fig|240292.3.peg.2655; -.
DR   HOGENOM; Q3MCT9; -.
DR   OMA; Q3MCT9; GPVEWLQ.
DR   BioCyc; AVAR240292:AVA_1574-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00323; -; 1.
DR   InterPro; IPR001015; Ferrochelatase.
DR   InterPro; IPR019772; Ferrochelatase_AS.
DR   PANTHER; PTHR11108; Ferrochelatase; 1.
DR   Pfam; PF00762; Ferrochelatase; 1.
DR   ProDom; PD002792; Ferrochelatase; 1.
DR   TIGRFAMs; TIGR00109; hemH; 1.
DR   PROSITE; PS00534; FERROCHELATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Heme biosynthesis; Iron; Lyase;
KW   Metal-binding; Porphyrin biosynthesis.
FT   CHAIN         1    388       Ferrochelatase.
FT                                /FTId=PRO_1000019272.
FT   METAL       196    196       Iron (By similarity).
FT   METAL       277    277       Iron (By similarity).
SQ   SEQUENCE   388 AA;  44129 MW;  A220751221FE742C CRC64;
     MGRVGVLLLN LGGPDKLEDV GPFLFNLFSD PEIIRLPFRW LQKPLAWFIA SRRTKTSQEN
     YKQIGGGSPL RRITEAQGEA LKEQLHDLGQ EANIYVGMRY WHPYTEEAIA LLTQDNLDNL
     VILPLYPQFS ISTSGSSFRL LERLWQEDPK LQRLDYTVIP SWYKEPCYLQ AMAELISQEV
     DQFPDPDQVH VFFSAHGVPK SYVEEAGDPY QQEIEECTAL IMQTLNRPNP HTLAYQSRVG
     PVEWLQPYTE DALKELGAQG VKDLVVVPIS FVSEHIETLQ EIDIEYREIA EEAGIHNFRR
     VAAPNTHPVF IRALANLVID ALNKPSFKLS QAAQIKKMVK MYPPESWEWG MTSSAEVWNG
     RIAMLGFIAL IIELVTGQGL LHMIGLLQ
//