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Database: UniProt
Entry: E8TGU9_MESCW
LinkDB: E8TGU9_MESCW
Original site: E8TGU9_MESCW 
ID   E8TGU9_MESCW            Unreviewed;       343 AA.
AC   E8TGU9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|HAMAP-Rule:MF_00218};
DE            Short=UPD {ECO:0000256|HAMAP-Rule:MF_00218};
DE            Short=URO-D {ECO:0000256|HAMAP-Rule:MF_00218};
DE            EC=4.1.1.37 {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|HAMAP-Rule:MF_00218};
GN   Name=hemE {ECO:0000256|HAMAP-Rule:MF_00218};
GN   OrderedLocusNames=Mesci_0869 {ECO:0000313|EMBL:ADV10035.1};
OS   Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS   WSM1271).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV10035.1, ECO:0000313|Proteomes:UP000007471};
RN   [1] {ECO:0000313|Proteomes:UP000007471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC   {ECO:0000313|Proteomes:UP000007471};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA   Tiwari R.P., Woyke T.;
RT   "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT   WSM1271.";
RL   Submitted (JAN-2011) 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:0000256|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:0000256|HAMAP-Rule:MF_00218,
CC         ECO:0000256|RuleBase:RU000554};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004804, ECO:0000256|HAMAP-Rule:MF_00218,
CC       ECO:0000256|RuleBase:RU000554}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_00218}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00218}.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009935, ECO:0000256|HAMAP-Rule:MF_00218,
CC       ECO:0000256|RuleBase:RU004169}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00218}.
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DR   EMBL; CP002447; ADV10035.1; -; Genomic_DNA.
DR   RefSeq; WP_013528730.1; NC_014923.1.
DR   RefSeq; YP_004140085.1; NC_014923.1.
DR   AlphaFoldDB; E8TGU9; -.
DR   STRING; 765698.Mesci_0869; -.
DR   KEGG; mci:Mesci_0869; -.
DR   PATRIC; fig|765698.3.peg.1296; -.
DR   eggNOG; COG0407; Bacteria.
DR   HOGENOM; CLU_040933_0_0_5; -.
DR   OrthoDB; 9806656at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000007471; 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   NCBIfam; TIGR01464; hemE; 1.
DR   PANTHER; PTHR21091; METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED; 1.
DR   PANTHER; PTHR21091:SF169; UROPORPHYRINOGEN DECARBOXYLASE; 1.
DR   Pfam; PF01208; URO-D; 1.
DR   SUPFAM; SSF51726; UROD/MetE-like; 1.
DR   PROSITE; PS00906; UROD_1; 1.
DR   PROSITE; PS00907; UROD_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00218};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00218};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00218};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00218}.
FT   DOMAIN          20..29
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00906"
FT   DOMAIN          138..154
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00907"
FT   BINDING         25..29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   SITE            75
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   343 AA;  37891 MW;  F6536DBB7F090CB0 CRC64;
     MPQNRIMLDV LKGKAHFPPP LWMMRQAGRY LPEYRETRRR AGSFLDLCYD PDLAVEVTLQ
     PIERFGFDAS ILFSDILVVP HALGRDVRFE EGRGPLLTPI TAPEILALEG KVFHVNLEPV
     YETVRRLRAK LPDETTLIGF CGAPWTVATY MIAGHGTPDQ APARLFAYRE PVAFQRLLKV
     LAEHSAAYLI RQIEAGADVV QIFDSWSGVL DDETFDLFCV QPMAEIVGRV RAVYPDVPII
     GFPKGAGSRY RTYRQKTGVT ALGIDWTVPL IAAKELQRSG AVQGNLDPLR LVAGGKALSD
     GVEAILRALG DGPLIFNLGH GITPETPIAH VEAMVKQVRS ATR
//
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