ID A0A2G5WPA0_9BACL Unreviewed; 347 AA. AC A0A2G5WPA0; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 07-NOV-2018, entry version 5. DE RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000256|HAMAP-Rule:MF_00218, ECO:0000256|RuleBase:RU000554, ECO:0000256|SAAS:SAAS01089773}; 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|HAMAP-Rule:MF_00218, ECO:0000256|RuleBase:RU000554, ECO:0000256|SAAS:SAAS01089758}; 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; OC 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, ECO:0000256|SAAS:SAAS01089770}. CC -!- CATALYTIC ACTIVITY: Uroporphyrinogen III = coproporphyrinogen + 4 CC CO(2). {ECO:0000256|HAMAP-Rule:MF_00218, CC ECO:0000256|RuleBase:RU000554, ECO:0000256|SAAS:SAAS01089769}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: CC step 4/4. {ECO:0000256|HAMAP-Rule:MF_00218, CC ECO:0000256|RuleBase:RU000554, ECO:0000256|SAAS:SAAS01089774}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00218, CC ECO:0000256|SAAS:SAAS01089757}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00218, CC ECO:0000256|SAAS:SAAS01089775}. CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family. CC {ECO:0000256|HAMAP-Rule:MF_00218, ECO:0000256|RuleBase:RU004169, CC ECO:0000256|SAAS:SAAS01097334}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00218}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 Complete proteome {ECO:0000313|Proteomes:UP000229695}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00218, KW ECO:0000256|SAAS:SAAS01089759}; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00218, KW ECO:0000256|RuleBase:RU000554, ECO:0000256|SAAS:SAAS01089764}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00218, ECO:0000256|RuleBase:RU000554, KW ECO:0000256|SAAS:SAAS01089761}; KW Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00218, KW ECO:0000256|RuleBase:RU000554, ECO:0000256|SAAS:SAAS01089766}. FT DOMAIN 21 30 Uroporphyrinogen_deCOase. FT {ECO:0000259|PROSITE:PS00906}. FT DOMAIN 139 155 Uroporphyrinogen_deCOase. FT {ECO:0000259|PROSITE:PS00907}. FT REGION 26 30 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00218}. FT BINDING 75 75 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00218}. FT BINDING 151 151 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00218}. FT BINDING 206 206 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00218}. FT BINDING 319 319 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00218}. FT SITE 75 75 Transition state stabilizer. FT {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 //