(data stored in ACNUC7421 zone)

SWISSPROT: DCUP_EDWI9

ID   DCUP_EDWI9              Reviewed;         354 AA.
AC   C5BHE8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 48.
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=NT01EI_0180;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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: Uroporphyrinogen III = coproporphyrinogen + 4
CC       CO(2). {ECO:0000255|HAMAP-Rule:MF_00218}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate:
CC       step 4/4. {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}.
DR   EMBL; CP001600; ACR67426.1; -; Genomic_DNA.
DR   RefSeq; WP_015869638.1; NC_012779.2.
DR   SMR; C5BHE8; -.
DR   STRING; 634503.NT01EI_0180; -.
DR   EnsemblBacteria; ACR67426; ACR67426; NT01EI_0180.
DR   GeneID; 7958771; -.
DR   KEGG; eic:NT01EI_0180; -.
DR   PATRIC; fig|634503.3.peg.162; -.
DR   eggNOG; ENOG4105CFZ; Bacteria.
DR   eggNOG; COG0407; LUCA.
DR   HOGENOM; HOG000253896; -.
DR   KO; K01599; -.
DR   OMA; SWAGQLS; -.
DR   OrthoDB; POG091H040E; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00717; URO-D; 1.
DR   HAMAP; MF_00218; URO_D; 1.
DR   InterPro; IPR006361; Uroporphyrinogen_deCO2ase_HemE.
DR   InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR   Pfam; PF01208; URO-D; 1.
DR   TIGRFAMs; TIGR01464; hemE; 1.
DR   PROSITE; PS00906; UROD_1; 1.
DR   PROSITE; PS00907; UROD_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHE8.
DR   SWISS-2DPAGE; C5BHE8.
KW   Complete proteome; Cytoplasm; Decarboxylase; Lyase;
KW   Porphyrin biosynthesis; Reference proteome.
FT   CHAIN         1    354       Uroporphyrinogen decarboxylase.
FT                                /FTId=PRO_1000204231.
FT   REGION       27     31       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   BINDING      77     77       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   BINDING     154    154       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   BINDING     209    209       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   BINDING     327    327       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00218}.
FT   SITE         77     77       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00218}.
SQ   SEQUENCE   354 AA;  39201 MW;  54521A596A53DB93 CRC64;
     MTELKNDRYL RALLRQPVDV TPVWMMRQAG RYLPEYNATR AQAGNFIALC KNAELACEVT
     LQPLRRFPLD AAILFSDILT VPDAMGLGLY FETGEGPRFT HSVTCHADIQ RLPIPDPEQE
     LGYVMDAVRT IRRSLRGDVP LIGFSGSPWT LATYMVEGGS SKAFTKIKKV MFSDPAALHL
     LLDKLAQSVI LYLNAQIRAG AQAVMIFDTW GGVLTGRDYR EFSLRYMHQI VDGLQRESEG
     RRVPVTLFTK GGGQWLEAMA DTGCDALGLD WTCDIADARR RVGGRVALQG NMDPSLLYAP
     PARIEQEVET ILAGFGQGEG HICNLGHGIH PDVPPKHAGV FVDAVHRLSV PYHR
//

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