DCUP_SHIFL
ID DCUP_SHIFL Reviewed; 354 AA.
AC Q83PB7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=SF4069, S3666;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
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; AE005674; AAN45498.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18703.1; -; Genomic_DNA.
DR RefSeq; NP_709791.1; NC_004337.2.
DR RefSeq; WP_000137636.1; NZ_WPGW01000040.1.
DR PDB; 3CYV; X-ray; 2.80 A; A=1-354.
DR PDBsum; 3CYV; -.
DR AlphaFoldDB; Q83PB7; -.
DR SMR; Q83PB7; -.
DR STRING; 198214.SF4069; -.
DR EnsemblBacteria; AAN45498; AAN45498; SF4069.
DR EnsemblBacteria; AAP18703; AAP18703; S3666.
DR GeneID; 1027590; -.
DR GeneID; 58390065; -.
DR KEGG; sfl:SF4069; -.
DR KEGG; sfx:S3666; -.
DR PATRIC; fig|198214.7.peg.4793; -.
DR HOGENOM; CLU_040933_0_0_6; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1104410at2; -.
DR UniPathway; UPA00251; UER00321.
DR EvolutionaryTrace; Q83PB7; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Decarboxylase; Lyase; Porphyrin biosynthesis;
KW Reference proteome.
FT CHAIN 1..354
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187638"
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 HELIX 8..13
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3CYV"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:3CYV"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:3CYV"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 175..198
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:3CYV"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:3CYV"
FT TURN 313..317
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3CYV"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 335..349
FT /evidence="ECO:0007829|PDB:3CYV"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:3CYV"
SQ SEQUENCE 354 AA; 39229 MW; 172465106DD068B3 CRC64;
MTELKNDRYL RALLRQPVDV TPVWMMRQAG RYLPEYKATR AQAGDFMSLC KNAELACEVT
LQPLRRYPLD AAILFSDILT VPDAMGLGLY FEAGEGPRFT SPVTCKADVD KLPIPDPEDE
LGYVMNAVRT IRHELKGEVP LIGFSGSPWT LATYMVEGGS SKAFTVIKKM MYADPQALHA
LLDKLAKSVT LYLNAQIKAG AQAVMIFDTW GGVLTGRDYQ QFSLYYMHKI VDGLLRENDG
RRVPVTLFTK GGGQWLEAMA ETGCDALGLD WTTDIADARR RVGNKVALQG NMDPSMLYAP
PARIEEEVAT ILAGFGHGEG HVFNLGHGIH QDVPPEHAGV FVEAVHRLSE QYHR
