HEMH_SYNSC
ID HEMH_SYNSC Reviewed; 391 AA.
AC Q3ALP2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Syncc9605_0716;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC Rule:MF_00323}.
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DR EMBL; CP000110; ABB34490.1; -; Genomic_DNA.
DR RefSeq; WP_011363718.1; NC_007516.1.
DR AlphaFoldDB; Q3ALP2; -.
DR SMR; Q3ALP2; -.
DR STRING; 110662.Syncc9605_0716; -.
DR EnsemblBacteria; ABB34490; ABB34490; Syncc9605_0716.
DR KEGG; syd:Syncc9605_0716; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_4_3_3; -.
DR OMA; LGDPYHC; -.
DR OrthoDB; 780534at2; -.
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;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis.
FT CHAIN 1..391
FT /note="Ferrochelatase"
FT /id="PRO_1000019381"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 281
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ SEQUENCE 391 AA; 43640 MW; 78717D0345EAD8DA CRC64;
MSRVGVVLLN LGGPERIQDV GPFLYNLFAD PEIIRLPSPA LQKPLAWLIS TLRSGKSQEA
YRSIGGGSPL RRITEQQARE LQSLLRQRGI DATSYVAMRY WHPFTESAVA DIKADGMDEV
VVLPLYPHFS ISTSGSSFRE LQRLRQADPA FEKLPIRCIR SWFDHPGYVK AMAELIAAEV
RNSDDPTKAH VFFSAHGVPK SYVEEAGDPY QKEIETCTGL IMKELAVQMG HDNPFTLAYQ
SRVGPVEWLK PYTEEALEEL GQAKTNDLVV VPISFVSEHI ETLEEIDIEY RELATEAGVV
NFRRVRALDT YAPFIEGLAD LVATSLQGPE VSLDAAAELP NKVKLYPQEK WEWGWNNSSE
VWNGRLAMVG FSAFLLELIS GQGPLHALGL L
