DCUP_SALPB
ID DCUP_SALPB Reviewed; 354 AA.
AC A9N0K9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=SPAB_05157;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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:
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; CP000886; ABX70438.1; -; Genomic_DNA.
DR RefSeq; WP_000137623.1; NC_010102.1.
DR AlphaFoldDB; A9N0K9; -.
DR SMR; A9N0K9; -.
DR KEGG; spq:SPAB_05157; -.
DR PATRIC; fig|1016998.12.peg.4831; -.
DR HOGENOM; CLU_040933_0_0_6; -.
DR OMA; LWLMRQA; -.
DR BioCyc; SENT1016998:SPAB_RS20990-MON; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000008556; 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..354
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_1000078085"
FT BINDING 27..31
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"
SQ SEQUENCE 354 AA; 39132 MW; 7122D53D98310CBB CRC64;
MTELKNDRYL RALLRQPVDV TPVWMMRQAG RYLPEYKATR AQAGDFMSLC KNAELACEVT
LQPLRRYPLD AAILFSDILT IPDAMGLGLY FEAGEGPRFT APVTCKADVE KLPIPDPEGE
LGYVMNAVRT IRRELKGEVP LIGFSGSPWT LATYMVEGGS SKAFTVIKKM MYADPQALHL
LLDKLAKSVT LYLNAQIKAG AQSVMIFDTW GGVLTGRDYQ QFSLYYMHKI VDGLLRENDG
RRVPVTLFTK GGGQWLEAMA ETGCDALGLD WTTDIADARR RVGHKVALQG NMDPSMLYAP
PARIEDEVAT ILAGFGQGEG HVFNLGHGIH QDVPPEHAGA FVEAVHRLSA QYHN
