HEMH_SYNP6
ID HEMH_SYNP6 Reviewed; 387 AA.
AC Q5N2B2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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}; OrderedLocusNames=syc1368_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(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. {ECO:0000255|HAMAP-
CC Rule:MF_00323}.
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DR EMBL; AP008231; BAD79558.1; -; Genomic_DNA.
DR RefSeq; WP_011243680.1; NC_006576.1.
DR AlphaFoldDB; Q5N2B2; -.
DR SMR; Q5N2B2; -.
DR STRING; 269084.syc1368_c; -.
DR EnsemblBacteria; BAD79558; BAD79558; syc1368_c.
DR KEGG; syc:syc1368_c; -.
DR eggNOG; COG0276; Bacteria.
DR OMA; LGDPYHC; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000001175; 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;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis.
FT CHAIN 1..387
FT /note="Ferrochelatase"
FT /id="PRO_0000175216"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 277
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ SEQUENCE 387 AA; 44294 MW; DBE58C11AE0DE78B CRC64;
MGRVGVLLLN LGGPERLEDV GPFLYNLFAD PEIIRLPFPW LQKPLAWLIS SLRTRKSQEN
YKQIGGGSPL RRITEEQATA LRQSLSDRGQ AAQVYIGMRY WHPFTEEAIA QIKADGIDRL
VILPLYPQFS ISTSGSSFRL LQRLRDRDPE FQKIDCSVVP SWYERSGYLQ AMAELIAQEL
DKLEQPEQGH VFFSAHGVPV SYVEEAGDPY QREIEDCTRK IMETLGRSNP WTLAYQSRVG
PVEWLQPYTE DALEELAERG VKDLVVVPIS FVSEHIETLE EIDIEYREIA EEAGIERFLR
VPALNTHPLF IQDLSDLVEQ TLEQPRFRLE DVTLLPKKVK LYPQERWEWG ITLNAEVWNG
RIAMLGFLAL LVELLTGRGP LHALGLL