DCUP2_ARATH
ID DCUP2_ARATH Reviewed; 394 AA.
AC O22886;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Uroporphyrinogen decarboxylase 2, chloroplastic;
DE Short=UPD2;
DE Short=URO-D2;
DE EC=4.1.1.37;
DE Flags: Precursor;
GN Name=HEME2; OrderedLocusNames=At2g40490; ORFNames=T2P4.16;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 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 [5]
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 -!- INDUCTION: Up-regulated by light. Not regulated by circadian rhythm.
CC {ECO:0000269|PubMed:15326282}.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AC002336; AAB87587.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09837.1; -; Genomic_DNA.
DR EMBL; AY142634; AAN13092.1; -; mRNA.
DR PIR; B84830; B84830.
DR RefSeq; NP_181581.1; NM_129611.5.
DR AlphaFoldDB; O22886; -.
DR SMR; O22886; -.
DR BioGRID; 3982; 13.
DR STRING; 3702.AT2G40490.1; -.
DR iPTMnet; O22886; -.
DR PaxDb; O22886; -.
DR PRIDE; O22886; -.
DR ProteomicsDB; 224586; -.
DR EnsemblPlants; AT2G40490.1; AT2G40490.1; AT2G40490.
DR GeneID; 818644; -.
DR Gramene; AT2G40490.1; AT2G40490.1; AT2G40490.
DR KEGG; ath:AT2G40490; -.
DR Araport; AT2G40490; -.
DR TAIR; locus:2061903; AT2G40490.
DR eggNOG; KOG2872; Eukaryota.
DR HOGENOM; CLU_040933_0_2_1; -.
DR InParanoid; O22886; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1114675at2759; -.
DR PhylomeDB; O22886; -.
DR BioCyc; ARA:AT2G40490-MON; -.
DR UniPathway; UPA00251; UER00321.
DR UniPathway; UPA00668; -.
DR PRO; PR:O22886; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22886; baseline and differential.
DR Genevisible; O22886; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; 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 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 Chlorophyll biosynthesis; Chloroplast; Decarboxylase; Lyase; Plastid;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..394
FT /note="Uroporphyrinogen decarboxylase 2, chloroplastic"
FT /id="PRO_0000036329"
FT BINDING 74..78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 124
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 394 AA; 43580 MW; B97992D4EE1AD9A7 CRC64;
MSILQVSTSS LSSSTLLSIS PRKSLSSTKS CRIVRCSVEG TTVTERKVSA TSEPLLLRAV
KGEVVDRPPV WLMRQAGRYM KSYQTLCEKY PSFRDRSENA DLVVEISLQP WKVFKPDGVI
LFSDILTPLS GMNIPFDIVK GKGPIIFNPP QSAADVAQVR EFVPEESVPY VGEALRRLRN
EVNNEAAVLG FVGAPFTLSS YVIEGGSSKN FTQIKRLAFS QPKVLHALLQ KFTTSMITYI
RYQADSGAQA VQIFDSWATE LSPVDFEEFS LPYLKQIVEA VKQTHPNLPL ILYASGSGGL
LERLARTGVD VVSLDWTVDM AEGRDRLGRD IAVQGNVDPG VLFGSKEFIT SRIHDTVKKA
GRDKHILNLG HGIKVGTPEE NVAHFFEVAQ EIRY
