HEMH_SALTY
ID HEMH_SALTY Reviewed; 320 AA.
AC P37408;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 128.
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}; Synonyms=visA;
GN OrderedLocusNames=STM0489;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
RC STRAIN=LT2;
RX PubMed=7814329; DOI=10.1128/jb.177.2.390-400.1995;
RA Gutierrez J.A., Csonka L.N.;
RT "Isolation and characterization of adenylate kinase (adk) mutations in
RT Salmonella typhimurium which block the ability of glycine betaine to
RT function as an osmoprotectant.";
RL J. Bacteriol. 177:390-400(1995).
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 -!- SUBUNIT: Monomer. {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; AE006468; AAL19443.1; -; Genomic_DNA.
DR EMBL; L26246; AAA65970.1; -; Genomic_DNA.
DR RefSeq; NP_459484.1; NC_003197.2.
DR RefSeq; WP_001250078.1; NC_003197.2.
DR AlphaFoldDB; P37408; -.
DR SMR; P37408; -.
DR STRING; 99287.STM0489; -.
DR PaxDb; P37408; -.
DR EnsemblBacteria; AAL19443; AAL19443; STM0489.
DR GeneID; 1252009; -.
DR KEGG; stm:STM0489; -.
DR PATRIC; fig|99287.12.peg.523; -.
DR HOGENOM; CLU_018884_0_0_6; -.
DR OMA; LGDPYHC; -.
DR PhylomeDB; P37408; -.
DR BioCyc; SENT99287:STM0489-MON; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000001014; 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..320
FT /note="Ferrochelatase"
FT /id="PRO_0000175197"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT CONFLICT 41
FT /note="P -> S (in Ref. 2; AAA65970)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="E -> Q (in Ref. 2; AAA65970)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="S -> C (in Ref. 2; AAA65970)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="R -> P (in Ref. 2; AAA65970)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="I -> M (in Ref. 2; AAA65970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35914 MW; F391D13736239817 CRC64;
MRQTKTGILL ANLGTPDAPT PEAVKRYLKQ FLSDRRVVDT PRLLWWPLLR GVILPLRSPR
VAKLYQSIWM DGGSPLMVYS REQQQALAAR LPDTPVALGM SYGSPSLESA VDELLASDVD
HIVVLPLYPQ YSCSTVGAVW DELGRILARK RRIPGISFIR DYADDGAYID ALAKSARESF
ARHGEPDVLL LSYHGIPQRY ADEGDDYPQR CRDTTRELVS ALGLPPEKVM MTFQSRFGRE
PWLTPYTDET LKMLGEKGTG HIQVMCPGFA ADCLETLEEI AEQNREIFLE AGGKKYAYIP
ALNATPEHID MMLKLTAPYR
