ID A0A1M6EKI5_9FLAO Unreviewed; 342 AA.
AC A0A1M6EKI5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN04488096_105122 {ECO:0000313|EMBL:SHI85760.1};
OS Mesonia phycicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mesonia.
OX NCBI_TaxID=579105 {ECO:0000313|EMBL:SHI85760.1, ECO:0000313|Proteomes:UP000184225};
RN [1] {ECO:0000313|EMBL:SHI85760.1, ECO:0000313|Proteomes:UP000184225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21425 {ECO:0000313|EMBL:SHI85760.1,
RC ECO:0000313|Proteomes:UP000184225};
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; FQYY01000005; SHI85760.1; -; Genomic_DNA.
DR RefSeq; WP_073150397.1; NZ_FQYY01000005.1.
DR AlphaFoldDB; A0A1M6EKI5; -.
DR STRING; 579105.SAMN04488096_105122; -.
DR OrthoDB; 9806656at2; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000184225; 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:UP000184225}.
FT DOMAIN 20..29
FT /note="Uroporphyrinogen decarboxylase (URO-D)"
FT /evidence="ECO:0000259|PROSITE:PS00906"
FT BINDING 25..29
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT SITE 74
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ SEQUENCE 342 AA; 38365 MW; 3AACBD2CD5D4FB6F CRC64;
MIKNDLFLKA LKGETVERPP VWMMRQAGRY LPDFMKLKEK YDFFTRCQTP ELATEITVMP
IKQVGTDAAI LFSDILVVPQ AMGIEIEMKP GVGPWLPTPI RTSAQVDNIV VPNVYEELGY
VYEAIKMTKQ ELNNEVPLIG FAGSPWTILC YLIQGQGSKN FDKAKEFCFT NPVAAHMLLQ
KITDTTIAYL KGKVEVGVDA VQLFDSWGGM LSPVDYQEFS WQYMQQIIDA LKEQIPVIAF
GKGCWFALKE MSQSGASALG VDWTCSAANA RYLSGGNITL QGNFDPSRLF SPPKEIKKMV
HQMINEFGKD KYIVNLGHGI LPNIPVENAK AFVEAVKEYQ PR
//
