DCUP_MYCGI
ID DCUP_MYCGI Reviewed; 354 AA.
AC A4TCS1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Mflv_3919;
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL Submitted (APR-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; CP000656; ABP46390.1; -; Genomic_DNA.
DR RefSeq; WP_011894770.1; NC_009338.1.
DR AlphaFoldDB; A4TCS1; -.
DR SMR; A4TCS1; -.
DR STRING; 350054.Mflv_3919; -.
DR EnsemblBacteria; ABP46390; ABP46390; Mflv_3919.
DR KEGG; mgi:Mflv_3919; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_1_11; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1104410at2; -.
DR UniPathway; UPA00251; UER00321.
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_1000078078"
FT BINDING 30..34
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 79
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 333
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT SITE 79
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ SEQUENCE 354 AA; 37531 MW; 13F5649F5E84E900 CRC64;
MNTRRELPES PYLAAAAGRK PHRVPVWMMR QAGRSLPEYR ELRAKNTMMQ ACFDADLITE
ITLQPVRRHG VDAAILFSDI VVPLRAAGID LDIVPDVGPV IAHPIRTAAD VATVSPLRRE
TVAPVATAIG QLTAALGDVA LIGFAGAPFT LASYLIEGGP SRNHERTKAM MLGETETWNA
LMAALTDVTI EFLRVQLDAG VDAIQVFDSW AGTLSLADYR AYVLPHSARV FEALAGYGVP
MTHFGVGTAE LLGAMSEAVS GHGVPAVVGV DWRTSLTDAA ARVRPGCALQ GNLDPVVLLA
GWPVVERAVR AVVEDGRRAV DAGATGHVFN LGHGVLPATD PAIITDAVAL VHQL