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Database: UniProt
Entry: A0A1M4W5D8_9BACT
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ID   A0A1M4W5D8_9BACT        Unreviewed;       382 AA.
AC   A0A1M4W5D8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   ORFNames=SAMN05443144_103127 {ECO:0000313|EMBL:SHE76481.1};
OS   Fodinibius roseus.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX   NCBI_TaxID=1194090 {ECO:0000313|EMBL:SHE76481.1, ECO:0000313|Proteomes:UP000184041};
RN   [1] {ECO:0000313|EMBL:SHE76481.1, ECO:0000313|Proteomes:UP000184041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21986 {ECO:0000313|EMBL:SHE76481.1,
RC   ECO:0000313|Proteomes:UP000184041};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FQUS01000003; SHE76481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M4W5D8; -.
DR   STRING; 1194090.SAMN05443144_103127; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000184041; Unassembled WGS sequence.
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.
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          57..66
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00906"
FT   BINDING         62..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   SITE            111
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   382 AA;  42897 MW;  7FA1213B9EA8F719 CRC64;
     MQRQAGRTIL QSSLLQLAFL IFKNLGQIKN SMKNAFPELK NDLLLRTLNG REVERPPVWM
     MRQAGRYLPQ YMEIRKKYTF FERVETPELA CEITIQPIDE LGPDAAIIFS DILTVPQALG
     IDVDLVKGKG PVIDNPIRSV DDAFAILARD VPGKLNHVME AITLTRRELN GRVPLIGFAG
     APWTLFCYMV QGEGSKNFAK AKAFMYQHPD AARHVMKELT KATIDYLKAQ VSAGAQVVQL
     FDSWAGLLGP EDFNEWAMPC LMEICDAVDE VPLILFAKGS WYALERLSFK SGAAAVGLDW
     TITPEYGREA TRGEIVLQGN FDPSKLMMPA DEIKRQTTRM IDRFGPQKYI ANLGHGILPN
     IPVDHARAFI DAVKEYEPRK VV
//
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