ID A0A2G5WPA0_9BACL Unreviewed; 347 AA. AC A0A2G5WPA0; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 29-SEP-2021, entry version 13. 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=CSV78_15490 {ECO:0000313|EMBL:PIC65875.1}; OS Sporosarcina sp. P16a. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina; OC unclassified Sporosarcina. OX NCBI_TaxID=2048262 {ECO:0000313|EMBL:PIC65875.1, ECO:0000313|Proteomes:UP000229695}; RN [1] {ECO:0000313|EMBL:PIC65875.1, ECO:0000313|Proteomes:UP000229695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P16a {ECO:0000313|EMBL:PIC65875.1, RC ECO:0000313|Proteomes:UP000229695}; RA Oliver A., Kay M., Cooper K.; RT "Comparative genomics and methylomics between geographically and RT phenotypically diverse Sporosarcina species."; RL Submitted (OCT-2017) 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|ARBA:ARBA00001082, ECO:0000256|HAMAP- CC Rule:MF_00218, 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}. 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:PIC65875.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PDYN01000030; PIC65875.1; -; Genomic_DNA. DR EnsemblBacteria; PIC65875; PIC65875; CSV78_15490. DR UniPathway; UPA00251; UER00321. DR Proteomes; UP000229695; 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 Pfam; PF01208; URO-D; 1. DR SUPFAM; SSF51726; SSF51726; 1. DR TIGRFAMs; TIGR01464; hemE; 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}. FT DOMAIN 21..30 FT /note="Uroporphyrinogen_deCOase" FT /evidence="ECO:0000259|PROSITE:PS00906" FT DOMAIN 139..155 FT /note="Uroporphyrinogen_deCOase" FT /evidence="ECO:0000259|PROSITE:PS00907" FT REGION 26..30 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218" FT BINDING 75 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218" FT BINDING 151 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218" FT BINDING 206 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218" FT BINDING 319 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218" FT SITE 75 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218" SQ SEQUENCE 347 AA; 38746 MW; 6327C4D905B4DB90 CRC64; MSTFNDTLLR AARGEEIEHT PVWFMRQAGR SQPEYLKIKE KYSLEEITHQ PELCAYVTKL PVDQYDVDAA ILYKDIVTPL VGIGVDVKIK PGVGPVISNP IRSAQDIANL GEFSAEEQVP YVLDTIKMLT QEQLNVPLIG FAGAPFTLAS YMIEGGPSKS YNLTKSFMVS EPQAWFALMD KLADMTISYI QAQVNAGVKA VQIFDSWVGA LNVSDYRIFI KPTMTRIFSE LRKLNVPLIT FGVGASHLAN EWHDLPVDVV GLDWRLSIKE AGERGMTKPV QGNLDPSMLL ADWSVIEERA KLIVEQGVEH GSHIFNLGHG VFPQVQPATL KRLTAFVHEY SRELRSK //