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DCUP_ECOLI
ID   DCUP_ECOLI              Reviewed;         354 AA.
AC   P29680; P78135; Q2M8T4;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 3.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000255|HAMAP-Rule:MF_00218};
DE            Short=UPD {ECO:0000255|HAMAP-Rule:MF_00218};
DE            Short=URO-D {ECO:0000255|HAMAP-Rule:MF_00218};
DE            EC=4.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00218};
GN   Name=hemE {ECO:0000255|HAMAP-Rule:MF_00218};
GN   OrderedLocusNames=b3997, JW3961;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=8224882; DOI=10.1016/0378-1119(93)90233-s;
RA   Nishimura K., Inokuchi H.;
RT   "Cloning and sequencing of the hemE gene encoding uroporphyrinogen III
RT   decarboxylase (UPD) from Escherichia coli K-12.";
RL   Gene 133:109-113(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT   from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC       uroporphyrinogen-III to yield coproporphyrinogen-III.
CC       {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen
CC         III; Xref=Rhea:RHEA:19865, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57308, ChEBI:CHEBI:57309; EC=4.1.1.37;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00218};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00218}.
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DR   EMBL; D12624; BAA02148.1; -; Genomic_DNA.
DR   EMBL; U00006; AAC43095.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76971.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77322.1; -; Genomic_DNA.
DR   PIR; H65206; H65206.
DR   RefSeq; NP_418425.1; NC_000913.3.
DR   RefSeq; WP_000137657.1; NZ_SSZK01000047.1.
DR   AlphaFoldDB; P29680; -.
DR   SMR; P29680; -.
DR   BioGRID; 4263218; 2.
DR   IntAct; P29680; 5.
DR   STRING; 511145.b3997; -.
DR   jPOST; P29680; -.
DR   PaxDb; P29680; -.
DR   PRIDE; P29680; -.
DR   EnsemblBacteria; AAC76971; AAC76971; b3997.
DR   EnsemblBacteria; BAE77322; BAE77322; BAE77322.
DR   GeneID; 66672091; -.
DR   GeneID; 948497; -.
DR   KEGG; ecj:JW3961; -.
DR   KEGG; eco:b3997; -.
DR   PATRIC; fig|1411691.4.peg.2714; -.
DR   EchoBASE; EB1505; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_0_6; -.
DR   InParanoid; P29680; -.
DR   OMA; LWLMRQA; -.
DR   PhylomeDB; P29680; -.
DR   BioCyc; EcoCyc:UROGENDECARBOX-MON; -.
DR   BioCyc; MetaCyc:UROGENDECARBOX-MON; -.
DR   UniPathway; UPA00251; UER00321.
DR   PRO; PR:P29680; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IMP:EcoCyc.
DR   GO; GO:0006785; P:heme B biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0006783; P:heme biosynthetic process; IMP:EcoliWiki.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:EcoliWiki.
DR   GO; GO:0019353; P:protoporphyrinogen IX biosynthetic process from glutamate; IMP:EcoCyc.
DR   GO; GO:0006780; P:uroporphyrinogen III biosynthetic process; IMP:EcoliWiki.
DR   CDD; cd00717; URO-D; 1.
DR   Gene3D; 3.20.20.210; -; 1.
DR   HAMAP; MF_00218; URO_D; 1.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   InterPro; IPR006361; Uroporphyrinogen_deCO2ase_HemE.
DR   InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR   Pfam; PF01208; URO-D; 1.
DR   SUPFAM; SSF51726; SSF51726; 1.
DR   TIGRFAMs; TIGR01464; hemE; 1.
DR   PROSITE; PS00906; UROD_1; 1.
DR   PROSITE; PS00907; UROD_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Lyase; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..354
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_0000187603"
FT   BINDING         27..31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   SITE            77
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   CONFLICT        72..78
FT                   /note="AILFSDI -> RSSFRY (in Ref. 1; BAA02148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83
FT                   /note="D -> I (in Ref. 1; BAA02148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        89..103
FT                   /note="LYFEAGEGPRFTSPV -> SSILKPEKVRVLPRQI (in Ref. 1;
FT                   BAA02148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251..256
FT                   /note="GGGQWL -> SATVA (in Ref. 1; BAA02148)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  39248 MW;  604933C50080260C CRC64;
     MTELKNDRYL RALLRQPVDV TPVWMMRQAG RYLPEYKATR AQAGDFMSLC KNAELACEVT
     LQPLRRYPLD AAILFSDILT VPDAMGLGLY FEAGEGPRFT SPVTCKADVD KLPIPDPEDE
     LGYVMNAVRT IRRELKGEVP LIGFSGSPWT LATYMVEGGS SKAFTVIKKM MYADPQALHA
     LLDKLAKSVT LYLNAQIKAG AQAVMIFDTW GGVLTGRDYQ QFSLYYMHKI VDGLLRENDG
     RRVPVTLFTK GGGQWLEAMA ETGCDALGLD WTTDIADARR RVGNKVALQG NMDPSMLYAP
     PARIEEEVAT ILAGFGHGEG HVFNLGHGIH QDVPPEHAGV FVEAVHRLSE QYHR
 
 
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