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Database: UniProt
Entry: A0A1C4D5I9_9BACT
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ID   A0A1C4D5I9_9BACT        Unreviewed;       343 AA.
AC   A0A1C4D5I9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=GA0116948_10585 {ECO:0000313|EMBL:SCC26694.1};
OS   Chitinophaga costaii.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1335309 {ECO:0000313|EMBL:SCC26694.1, ECO:0000313|Proteomes:UP000242818};
RN   [1] {ECO:0000313|EMBL:SCC26694.1, ECO:0000313|Proteomes:UP000242818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A37T2 {ECO:0000313|EMBL:SCC26694.1,
RC   ECO:0000313|Proteomes:UP000242818};
RA   Seilhamer J.J.;
RL   Submitted (AUG-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; FMAR01000005; SCC26694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4D5I9; -.
DR   STRING; 1335309.GA0116948_10585; -.
DR   OrthoDB; 9806656at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000242818; 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}; Reference proteome {ECO:0000313|Proteomes:UP000242818}.
FT   DOMAIN          22..31
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00906"
FT   BINDING         27..31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         208
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            76
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   343 AA;  38046 MW;  041450597A933A68 CRC64;
     MSALKNNLLL QALRGEKTSR TPVWMMRQAG RFLPDYIKLR DKYSFFERCQ TPELATEITV
     MPVDQVGVDA AILFSDILVV PQAMGLEVQL IEKLGPLLPH PIKTAEDLKR IQVPDVNDRL
     SYVFEALQLI KKTLNGRVPL IGFAGAPFTI LCYMVQGKGS KTFDEAKGFC FQQPAVAHAL
     LQMITDTTIA YLREQIRSGA DTVQIFDSWG GLLSPHDFEN FSLQYIRQIV AALKDIAPVI
     VFAKGAWFAL EEMAATGASG LGIDWGIKPQ LARQMAGSQV TLQGNFDPAN LLAPIPEIEK
     ATKRMLQEFG PHRHIANLGH GILPNVPVDH ARAFVETIKA YQH
//
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