DCUP_RICM5
ID DCUP_RICM5 Reviewed; 346 AA.
AC A8F331;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
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=RMA_1389;
OS Rickettsia massiliae (strain Mtu5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=416276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mtu5;
RX PubMed=17916642; DOI=10.1101/gr.6742107;
RA Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT "Lateral gene transfer between obligate intracellular bacteria: evidence
RT from the Rickettsia massiliae genome.";
RL Genome Res. 17:1657-1664(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABV85317.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000683; ABV85317.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041404921.1; NC_009900.1.
DR AlphaFoldDB; A8F331; -.
DR SMR; A8F331; -.
DR EnsemblBacteria; ABV85317; ABV85317; RMA_1389.
DR KEGG; rms:RMA_1389; -.
DR HOGENOM; CLU_040933_0_0_5; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000001311; 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..346
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000325687"
FT BINDING 21..25
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT SITE 71
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
SQ SEQUENCE 346 AA; 39981 MW; F864ADFDAED68E67 CRC64;
MKQIINPLKG NDNKIPIWFM RQAGRYLPEY KKVRETTKNF LDFCYDVNKA TEVTLQPIKR
YGFDAAIIFS DILVLPHAFG WEVDFKENIG PILKQFKSQE DFKYLQINPN DKLEKVYEII
KKVKKELPSP TSLIGFAGSP WTVMSYMLEG KGKQDFKTSK KFIYENKILA EELLNFITEK
TADHLINQAK SGVDVLKLFD SWSGVLAEEE FTEFVIEPTK KIVLKVKEVF PKTPIIAFPK
GAGLLYEKFI KEVPIDILAV DQMVPLEKMK EWSDKVIVQG NLDPVVLLTN KEIIKEKTYK
ILQAMKGKNF IFNLGHGILP ETPTENVEFL TEYVRLYEEK NSNSTF
