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DCUP_CHLAB
ID   DCUP_CHLAB              Reviewed;         333 AA.
AC   Q5L510;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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}; OrderedLocusNames=CAB844;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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; CR848038; CAH64285.1; -; Genomic_DNA.
DR   RefSeq; WP_011097371.1; NC_004552.2.
DR   AlphaFoldDB; Q5L510; -.
DR   SMR; Q5L510; -.
DR   EnsemblBacteria; CAH64285; CAH64285; CAB844.
DR   KEGG; cab:CAB844; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_0_0; -.
DR   OMA; LWLMRQA; -.
DR   OrthoDB; 1104410at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000001012; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
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.
FT   CHAIN           1..333
FT                   /note="Uroporphyrinogen decarboxylase"
FT                   /id="PRO_1000023894"
FT   BINDING         21..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT   SITE            70
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   333 AA;  37315 MW;  CAEECE06E91663CF CRC64;
     MSKFYDVIKP KASRPPVWFL RQVGRYMPQY RELKGSQTLK DFFHNTEAIT EATLLGPSLL
     KVDAAILFAD ILSLLDGFNI SYDFAPGPQI SFSPKEELIF TNDPQDTFSY LLKAIKNLVK
     RLSVPLIAFA ASPFTMACYL LEGGASKDFP KTMAFLYQHP ERFDALLKQL AEATVIYLKE
     QIQAGASAIQ LFESSSLRLP SALFSRYVTR PNTQLITQLK NSVSSPISLF CRCFDENFID
     LYSTGADTLH PDYHVNLSQI YTAVTHPGSL QGNIDPALFL LPQDQFLNHL EKYLSVLKHQ
     PKYIFNSGHG ILPETPLENV QAAVLCLTSI STS
 
 
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