ID DCUP1_ARATH Reviewed; 418 AA. AC Q93ZB6; Q9LKB1; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 2. DT 23-FEB-2022, entry version 128. DE RecName: Full=Uroporphyrinogen decarboxylase 1, chloroplastic; DE Short=UPD1; DE Short=URO-D1; DE EC=4.1.1.37; DE Flags: Precursor; GN Name=HEME1; OrderedLocusNames=At3g14930; ORFNames=K15M2.7; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10907853; DOI=10.1093/dnares/7.3.217; RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC RT clones."; RL DNA Res. 7:217-221(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=cv. Columbia; RX PubMed=14993207; DOI=10.1101/gr.1515604; RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., RA Weissenbach J., Salanoubat M.; RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a RT combined approach to evaluate and improve Arabidopsis genome annotation."; RL Genome Res. 14:406-413(2004). RN [5] RP IDENTIFICATION. RX PubMed=12777052; DOI=10.1023/a:1023005504702; RA Lange B.M., Ghassemian M.; RT "Genome organization in Arabidopsis thaliana: a survey for genes involved RT in isoprenoid and chlorophyll metabolism."; RL Plant Mol. Biol. 51:925-948(2003). RN [6] RP INDUCTION BY LIGHT. RX PubMed=15326282; DOI=10.1104/pp.104.042408; RA Matsumoto F., Obayashi T., Sasaki-Sekimoto Y., Ohta H., Takamiya K., RA Masuda T.; RT "Gene expression profiling of the tetrapyrrole metabolic pathway in RT Arabidopsis with a mini-array system."; RL Plant Physiol. 135:2379-2391(2004). CC -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of CC uroporphyrinogen-III to yield coproporphyrinogen-III. {ECO:0000250}. 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 -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll CC biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q93ZB6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q93ZB6-2; Sequence=VSP_037402; CC -!- INDUCTION: Up-regulated by light. Not regulated by circadian rhythm. CC {ECO:0000269|PubMed:15326282}. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BX824686; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305}; 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; AP000370; BAA97056.1; -; Genomic_DNA. DR EMBL; CP002686; AEE75589.1; -; Genomic_DNA. DR EMBL; CP002686; AEE75590.1; -; Genomic_DNA. DR EMBL; CP002686; AEE75591.1; -; Genomic_DNA. DR EMBL; AY057663; AAL15294.1; -; mRNA. DR EMBL; AY136476; AAM97141.1; -; mRNA. DR EMBL; BT008826; AAP68265.1; -; mRNA. DR EMBL; BX824686; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; NP_566495.1; NM_112355.3. [Q93ZB6-1] DR RefSeq; NP_850587.1; NM_180256.2. [Q93ZB6-1] DR RefSeq; NP_974316.1; NM_202587.1. [Q93ZB6-2] DR SMR; Q93ZB6; -. DR BioGRID; 6056; 5. DR STRING; 3702.AT3G14930.2; -. DR MetOSite; Q93ZB6; -. DR PaxDb; Q93ZB6; -. DR PRIDE; Q93ZB6; -. DR ProteomicsDB; 224608; -. [Q93ZB6-1] DR EnsemblPlants; AT3G14930.1; AT3G14930.1; AT3G14930. [Q93ZB6-1] DR EnsemblPlants; AT3G14930.2; AT3G14930.2; AT3G14930. [Q93ZB6-1] DR EnsemblPlants; AT3G14930.3; AT3G14930.3; AT3G14930. [Q93ZB6-2] DR GeneID; 820722; -. DR Gramene; AT3G14930.1; AT3G14930.1; AT3G14930. [Q93ZB6-1] DR Gramene; AT3G14930.2; AT3G14930.2; AT3G14930. [Q93ZB6-1] DR Gramene; AT3G14930.3; AT3G14930.3; AT3G14930. [Q93ZB6-2] DR KEGG; ath:AT3G14930; -. DR Araport; AT3G14930; -. DR TAIR; locus:2086300; AT3G14930. DR eggNOG; KOG2872; Eukaryota. DR HOGENOM; CLU_040933_0_2_1; -. DR InParanoid; Q93ZB6; -. DR OMA; TIDMEDG; -. DR OrthoDB; 1114675at2759; -. DR PhylomeDB; Q93ZB6; -. DR BioCyc; ARA:AT3G14930-MONOMER; -. DR UniPathway; UPA00251; UER00321. DR UniPathway; UPA00668; -. DR PRO; PR:Q93ZB6; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q93ZB6; baseline and differential. DR Genevisible; Q93ZB6; AT. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR. DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR. 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 2: Evidence at transcript level; KW Alternative splicing; Chlorophyll biosynthesis; Chloroplast; Decarboxylase; KW Lyase; Plastid; Porphyrin biosynthesis; Reference proteome; KW Transit peptide. FT TRANSIT 1..53 FT /note="Chloroplast" FT /evidence="ECO:0000305" FT CHAIN 54..418 FT /note="Uroporphyrinogen decarboxylase 1, chloroplastic" FT /id="PRO_0000376071" FT REGION 80..84 FT /note="Substrate binding" FT /evidence="ECO:0000250" FT BINDING 99 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 129 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 130 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 206 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 261 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 376 FT /note="Substrate" FT /evidence="ECO:0000250" FT SITE 130 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT VAR_SEQ 1..77 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14993207" FT /id="VSP_037402" FT CONFLICT 36 FT /note="V -> G (in Ref. 3; AAL15294)" FT /evidence="ECO:0000305" SQ SEQUENCE 418 AA; 46254 MW; F8A78980A6B08CB2 CRC64; MSLSSPTSAC SSSRCYSSGL SFPIGFGSNP INVGLVCYPK RYSIAARKFV VACSSSSSDP LLVKAAKGQA ISRPPAWMMR QAGRYMAVYQ KLAKKHPSFR ERSENTDLIV EISLQPWQAF RPDGVIIFSD ILTPLPAFGV PFDIEEVKGP VIQSPIRTEE DMKRLHPIDF EKLQFVGDSL KILRREVGEH AAVLGFVGAP WTIATYIVEG GTTRTYTVIK NMCHTAPDVL RALLSHLTKA ITEYVVYQVE HGAHCIQIFD SWGGQLTPEM WERWSKPYIE EIIHAVKKRC PDTPIVFYIN GNGGLLERMK GTGADVIGLD WTVDMADGRR RLGSEVSVQG NVDPAYLFSP LPALTEEIER VVKCAGPKGH ILNLGHGVLV GTPEEAVAHF FETARNLDYQ TLFQNHVPAE KAEPELVV //