HEMH1_SHEON
ID HEMH1_SHEON Reviewed; 334 AA.
AC Q8EFF4;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ferrochelatase 1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE EC=4.99.1.1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Heme synthase 1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Protoheme ferro-lyase 1 {ECO:0000255|HAMAP-Rule:MF_00323};
GN Name=hemH1 {ECO:0000255|HAMAP-Rule:MF_00323}; Synonyms=hemH-1;
GN OrderedLocusNames=SO_2019;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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, ECO:0000305}.
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DR EMBL; AE014299; AAN55069.2; -; Genomic_DNA.
DR RefSeq; NP_717625.2; NC_004347.2.
DR AlphaFoldDB; Q8EFF4; -.
DR SMR; Q8EFF4; -.
DR STRING; 211586.SO_2019; -.
DR PaxDb; Q8EFF4; -.
DR KEGG; son:SO_2019; -.
DR PATRIC; fig|211586.12.peg.1938; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_0_0_6; -.
DR OrthoDB; 780534at2; -.
DR PhylomeDB; Q8EFF4; -.
DR BioCyc; SONE211586:G1GMP-1861-MON; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..334
FT /note="Ferrochelatase 1"
FT /id="PRO_0000175198"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 282
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ SEQUENCE 334 AA; 37370 MW; 30CFD94E48A2DBB3 CRC64;
MTSPSPAFGV LLVNLGTPDE PTPKAVKRFL KQFLSDPRVV DLSPWLWQPI LQGIILNTRP
KKVAKLYQSV WTEQGSPLMV ISQCQAQKLA TDLSATFNQT IPVELGMSYG NPSIESGFAK
LKAQGAERIV VLPLYPQYSC STVASVFDAV AHYLTRVRDI PELRFNKQYF AHEAYIAALA
HSVKRHWKTH GQAEKLILSF HGIPLRYATE GDPYPEQCRT TAKLLAQALG LTDGQWQVCF
QSRFGKEEWL TPYADELLAD LPRQGVKSVD VICPAFATDC LETLEEISIG AKETFLHAGG
EAYHFIPCLN DDELHIELLR LLVQEQTQSW ISAE