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Database: UniProt
Entry: A0A2U1K3Q6_9BACI
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ID   A0A2U1K3Q6_9BACI        Unreviewed;       344 AA.
AC   A0A2U1K3Q6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=DCC39_09050 {ECO:0000313|EMBL:PWA11779.1};
OS   Pueribacillus theae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pueribacillus.
OX   NCBI_TaxID=2171751 {ECO:0000313|EMBL:PWA11779.1, ECO:0000313|Proteomes:UP000245998};
RN   [1] {ECO:0000313|EMBL:PWA11779.1, ECO:0000313|Proteomes:UP000245998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T8 {ECO:0000313|EMBL:PWA11779.1,
RC   ECO:0000313|Proteomes:UP000245998};
RA   Niu L.;
RT   "Camelliibacillus theae gen. nov., sp. nov., isolated from Pu'er tea.";
RL   Submitted (APR-2018) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWA11779.1}.
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DR   EMBL; QCZG01000016; PWA11779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1K3Q6; -.
DR   OrthoDB; 9806656at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000245998; 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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000245998}.
FT   DOMAIN          21..30
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00906"
FT   DOMAIN          140..156
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00907"
FT   BINDING         26..30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         207
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            77
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   344 AA;  39291 MW;  8A9C0721C7146447 CRC64;
     MTKFNDTFLK ACRGEQTDYV PVWFMRQAGR TQPEYLKIKE KYSLFEITHQ PELCARVTRL
     PIDEYNYGVD AAILYKDIMT PLPAIGVDVE IKPGAGPVIA NPIRSKQDVE RLGEIDPEND
     VDYILDTIKL LREQLTVPLI GFSGAPFTLA SYMIEGGSSR NYHKTKAFMH GEPEAWFMLM
     DKLGDMVISY VRAQIKAGAQ AIQIFDSWVG AVNRQDYRKY MKPVMERIFN ELRVEGVPLI
     MFGVGASHLA EEWADLPLDV VGLDWRLQIK EAREKGITKA LQGNLDPSFL LAPWPVIEEE
     VKRILDQGME QPGYIFNLGH GVFPEVNYKT LKRLAEFVHE YTLR
//
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