HEMH_CAUVC
ID HEMH_CAUVC Reviewed; 347 AA.
AC P57777;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=CC_3762;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF IRON-SULFUR
RP CLUSTER.
RX PubMed=11948160; DOI=10.1128/jb.184.9.2460-2464.2002;
RA Dailey T.A., Dailey H.A.;
RT "Identification of [2Fe-2S] clusters in microbial ferrochelatases.";
RL J. Bacteriol. 184:2460-2464(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- SUBUNIT: Homodimer.
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; AF184071; AAG12242.1; -; Genomic_DNA.
DR EMBL; AE005673; AAK25724.1; -; Genomic_DNA.
DR PIR; H87715; H87715.
DR RefSeq; NP_422556.1; NC_002696.2.
DR RefSeq; WP_010921589.1; NC_002696.2.
DR AlphaFoldDB; P57777; -.
DR SMR; P57777; -.
DR STRING; 190650.CC_3762; -.
DR EnsemblBacteria; AAK25724; AAK25724; CC_3762.
DR KEGG; ccr:CC_3762; -.
DR PATRIC; fig|190650.5.peg.3764; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_4_1_5; -.
DR OMA; FSYHGVP; -.
DR BioCyc; CAULO:CC3762-MON; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Heme biosynthesis; Iron; Iron-sulfur; Lyase;
KW Metal-binding; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..347
FT /note="Ferrochelatase"
FT /id="PRO_0000175126"
FT BINDING 158
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 332
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 339
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 341
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
SQ SEQUENCE 347 AA; 37121 MW; E666EAFBF8269809 CRC64;
MTQKLAVVLF NLGGPDGPDA VRPFLFNLFR DPAIIGAPAL IRYPLAALIS TTREKSAKAN
YAIMGGGSPL LPETEKQARA LEAALALAMP GVEAKCFIAM RYWHPLTDET ARQVAAFAPD
QVVLLPLYPQ FSTTTTGSSL KAWKKTYKGS GVQTTVGCYP TEGGLIEAHA RMIRESWEKA
GSPTNIRLLF SAHGLPEKVI LAGDPYQKQV EATAAAVAAH LPPQIEWTVC YQSRVGPLKW
IGPSTDDEIR RAGGEDKGVM ITPIAFVSEH VETLVELDHE YAELAEEVGA APYLRVSALG
TAPEFIDGLA KAVRDSVGKA PGTVSSACGW RCGADWSKCP CREGASA
