ID T0DN60_ALIAG Unreviewed; 344 AA.
AC T0DN60; A0A9E7CQN2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
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 ECO:0000313|EMBL:UNO48159.1};
GN ORFNames=K1I37_15955 {ECO:0000313|EMBL:UNO48159.1};
OS Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS / NCIMB 13137 / GD3B).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1356854 {ECO:0000313|EMBL:UNO48159.1, ECO:0000313|Proteomes:UP000829401};
RN [1] {ECO:0000313|Proteomes:UP000829401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3922 {ECO:0000313|Proteomes:UP000829401};
RX PubMed=36240455; DOI=10.1093/g3journal/jkac225;
RA Leonardo I.C., Barreto Crespo M.T., Gaspar F.B.;
RT "Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris
RT DSM 3922T, a taint-producing strain.";
RL G3 (Bethesda) 12:0-0(2022).
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; CP080467; UNO48159.1; -; Genomic_DNA.
DR RefSeq; WP_021295069.1; NZ_AURB01000035.1.
DR STRING; 1356854.N007_02400; -.
DR KEGG; aaco:K1I37_15955; -.
DR Proteomes; UP000829401; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-UniRule.
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:UP000829401}.
FT BINDING 24..28
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT SITE 73
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ SEQUENCE 344 AA; 38352 MW; C8EA0493D4F87BE1 CRC64;
MFNDTFLRAC RREKTATVPV WFMRQAGRYD ADYRAIRERY SLVEICEHPE VCVEVTKMPV
EKLGVDAAIL FSDIMIPVGA MGLPFEIREH VGPIIATPIR HERDVERLEV FDAKEKLPHV
LQTIERLASE LTVPLIGFVG GPFTLASYMI EGGPSRDYLK TKQMMVARPE LWQKLMDKLA
DMVIRYAGEQ VQAGAQALQV FDSWVGSLAP SDFVQYVKPT MQRIFAGLQP LGVPLIYFGV
NTGELLGEFA TTGANVIGVD WRVPLANARQ RVGSDVALQG NFDPAMLFAP AAEMKRRAID
ILQQGTKDPG FIFNLGHGVK PTTDIAALKY LVDVVHEFDV NRGV
//
