HEMH2_SHEON
ID HEMH2_SHEON Reviewed; 327 AA.
AC Q8EBZ7;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ferrochelatase 2 {ECO:0000255|HAMAP-Rule:MF_00323};
DE EC=4.99.1.1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Heme synthase 2 {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Protoheme ferro-lyase 2 {ECO:0000255|HAMAP-Rule:MF_00323};
GN Name=hemH2 {ECO:0000255|HAMAP-Rule:MF_00323}; Synonyms=hemH-2;
GN OrderedLocusNames=SO_3348;
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; AAN56346.1; -; Genomic_DNA.
DR RefSeq; NP_718902.1; NC_004347.2.
DR RefSeq; WP_011073218.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EBZ7; -.
DR SMR; Q8EBZ7; -.
DR STRING; 211586.SO_3348; -.
DR PaxDb; Q8EBZ7; -.
DR KEGG; son:SO_3348; -.
DR PATRIC; fig|1028802.3.peg.1931; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_0_0_6; -.
DR OMA; FSYHGVP; -.
DR OrthoDB; 780534at2; -.
DR PhylomeDB; Q8EBZ7; -.
DR BioCyc; SONE211586:G1GMP-3116-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..327
FT /note="Ferrochelatase 2"
FT /id="PRO_0000175199"
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 327 AA; 36398 MW; D098A1901F24171A CRC64;
MGHAARGKVG VLLLNLGTPD APTASAVRRY LAEFLSDPRV VEIPKLLWML ILYGIVLRVR
PAKSAALYQK VWTEAGSPLM DISLRQTAKL SDKLTADGHQ VSVHLAMRYG NPSVASTLRE
MHKQGIDKLV VLPLYPQYAA PTTGSAFDAI AKELSQWRYL PSLHFINTYH DNPDFIAALV
NSIRDDFDKH GKPQKLVLSY HGMPERNLHL GDPYYCFCMK TTRLVAEQLG LSKDEFAITF
QSRFGKAKWL QPYTDATMAA LPSQGVRDVA IVCPAFSADC LETLEEIVGE NGHIFTHAGG
EKFRYIPALN DNDDHIAMMA NLVKPYL
