HEMH_THEAC
ID HEMH_THEAC Reviewed; 308 AA.
AC Q9HLB8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Ta0311;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445063; CAC11456.1; -; Genomic_DNA.
DR RefSeq; WP_010900740.1; NC_002578.1.
DR AlphaFoldDB; Q9HLB8; -.
DR SMR; Q9HLB8; -.
DR STRING; 273075.Ta0311; -.
DR EnsemblBacteria; CAC11456; CAC11456; CAC11456.
DR GeneID; 1455934; -.
DR KEGG; tac:Ta0311; -.
DR eggNOG; arCOG05373; Archaea.
DR HOGENOM; CLU_018884_2_1_2; -.
DR OMA; LGDPYHC; -.
DR OrthoDB; 85754at2157; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000001024; 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; IPR033644; Ferrochelatase_C.
DR InterPro; IPR033659; Ferrochelatase_N.
DR PANTHER; PTHR11108; PTHR11108; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..308
FT /note="Ferrochelatase"
FT /id="PRO_0000175237"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ SEQUENCE 308 AA; 35241 MW; BF269B21A9C8F076 CRC64;
MKSALLLLSY GSPERIEDLD EYLKNIFNGK PVPESVREEN LRKYEMFGGR SPSNRIIESI
ARKLHEKIGD DMDVILAYKH WNPSIEEAVK GLGSYDNIVA IPLFSFYSQN VKDSYLNPLE
SALRRYGFSP RLEFVNGLAN SDLFLPMWAN IISEDASEDS FYLFDAHSLP APDREEDYLF
WLRYSTYKIS QILGLSRSDF GFQGGHLGWL GPSIYDVLNR IDASKITVIP ISFLYDHLEI
LYDLDYEFRK AVEAKGMHYR RVRMPNDSAM MVNMIERAAR SAITHLSGEK INGSIIGQPR
IADTDNGR
