位置:首页 > 蛋白库 > HEMH_YERPS
HEMH_YERPS
ID   HEMH_YERPS              Reviewed;         320 AA.
AC   Q05338; Q66DP6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 123.
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=YPTB0997;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-320.
RX   PubMed=8444803; DOI=10.1128/jb.175.5.1412-1422.1993;
RA   Kessler A.C., Haase A., Reeves P.R.;
RT   "Molecular analysis of the 3,6-dideoxyhexose pathway genes of Yersinia
RT   pseudotuberculosis serogroup IIA.";
RL   J. Bacteriol. 175:1412-1422(1993).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX936398; CAH20237.1; -; Genomic_DNA.
DR   EMBL; AF461770; AAB49397.1; -; Genomic_DNA.
DR   PIR; A47070; A47070.
DR   RefSeq; WP_002208599.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q05338; -.
DR   SMR; Q05338; -.
DR   EnsemblBacteria; CAH20237; CAH20237; YPTB0997.
DR   GeneID; 66842577; -.
DR   KEGG; yps:YPTB0997; -.
DR   OMA; LGDPYHC; -.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000001011; 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; 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.
FT   CHAIN           1..320
FT                   /note="Ferrochelatase"
FT                   /id="PRO_0000175235"
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"
SQ   SEQUENCE   320 AA;  36185 MW;  8CDFE94DAF266819 CRC64;
     MMQSKPGVLM VNLGTPDAPT SKAIKRYLAE FLSDRRVVDT SPLLWWPLLH GVILPLRSPR
     VAKLYQSVWM EEGSPLLVYS RRQQKALAAR MPDIPVELGM SYGSPNLPEA IEKLLAQGVT
     NLVILPLYPQ YSCSTSAAVW DAVARVLKGY RRLPSISFIR DYAEHPAYIS ALKQSVERSF
     AEHGQPDRLV MSFHGIPKRY AQLGDDYPIR CEDTSRALRA ALPLPAEKII MTYQSRFGRE
     PWLTPYTDET LKSLPSQGVK HIQLICPGFS ADCLETLEEI KEQNREFFLH AGGEKFEYIP
     ALNDDEGHIA LLEQLIRHNI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024