DCUP_TOBAC
ID DCUP_TOBAC Reviewed; 391 AA.
AC Q42967;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Uroporphyrinogen decarboxylase, chloroplastic;
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37;
DE Flags: Precursor;
GN Name=DCUP;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. SR1; TISSUE=Leaf;
RX PubMed=7599310; DOI=10.1007/bf00020244;
RA Mock H.-P., Trainotti L., Kruse E., Grimm B.;
RT "Isolation, sequencing and expression of cDNA sequences encoding
RT uroporphyrinogen decarboxylase from tobacco and barley.";
RL Plant Mol. Biol. 28:245-256(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 39-391, SUBUNIT, AND REACTION
RP MECHANISM.
RX PubMed=11524417; DOI=10.1074/jbc.m104759200;
RA Martins B.M., Grimm B., Mock H.-P., Huber R., Messerschmidt A.;
RT "Crystal structure and substrate binding modeling of the uroporphyrinogen-
RT III decarboxylase from Nicotiana tabacum. Implications for the catalytic
RT mechanism.";
RL J. Biol. Chem. 276:44108-44116(2001).
CC -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC uroporphyrinogen-III to yield coproporphyrinogen-III.
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11524417}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; X82833; CAA58040.1; -; mRNA.
DR PIR; S55732; S55732.
DR RefSeq; NP_001312840.1; NM_001325911.1.
DR PDB; 1J93; X-ray; 2.30 A; A=39-391.
DR PDBsum; 1J93; -.
DR AlphaFoldDB; Q42967; -.
DR SMR; Q42967; -.
DR STRING; 4097.Q42967; -.
DR ProMEX; Q42967; -.
DR GeneID; 107813684; -.
DR KEGG; nta:107813684; -.
DR BioCyc; MetaCyc:MON-11784; -.
DR UniPathway; UPA00251; UER00321.
DR EvolutionaryTrace; Q42967; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Chlorophyll biosynthesis; Chloroplast; Decarboxylase; Lyase;
KW Plastid; Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..391
FT /note="Uroporphyrinogen decarboxylase, chloroplastic"
FT /id="PRO_0000036331"
FT BINDING 71..75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 121
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:1J93"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:1J93"
FT TURN 90..95
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1J93"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 219..242
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1J93"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 336..340
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 343..357
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:1J93"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:1J93"
FT HELIX 376..387
FT /evidence="ECO:0007829|PDB:1J93"
SQ SEQUENCE 391 AA; 43116 MW; ABDE69205918AE79 CRC64;
MMSCNYSFSS ISPSSKSAFT SPSNFNLNPR LICCSAGGTV AEPKAINATQ PLLLDAVRGK
EVERPPVWLM RQAGRYMKSY QLLCEKYPLF RDRSENVDLV VEISLQPWKV FRPDGVILFS
DILTPLSGMN IPFDIIKGKG PVIFDPLRTA ADVEKVREFI PEKSVPYVGE ALTILRKEVN
NQAAVLGFVG APFTLASYVV EGGSSKNFTK IKRLAFAEPK VLHALLQKFA TSMAKYIRYQ
ADSGAQAVQI FDSWATELSP VDFEEFSLPY LKQIVDSVKL THPNLPLILY ASGSGGLLER
LPLTGVDVVS LDWTVDMADG RRRLGPNVAI QGNVDPGVLF GSKEFITNRI NDTVKKAGKG
KHILNLGHGI KVGTPEENFA HFFEIAKGLR Y
