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Database: UniProt
Entry: A0A2V0PRA2_9CHLO
LinkDB: A0A2V0PRA2_9CHLO
Original site: A0A2V0PRA2_9CHLO 
ID   A0A2V0PRA2_9CHLO        Unreviewed;       405 AA.
AC   A0A2V0PRA2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|RuleBase:RU000554};
DE            EC=4.1.1.37 {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|RuleBase:RU000554};
GN   ORFNames=Rsub_13395 {ECO:0000313|EMBL:GBG00641.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBG00641.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBG00641.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBG00641.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC       uroporphyrinogen-III to yield coproporphyrinogen-III.
CC       {ECO:0000256|ARBA:ARBA00002448}.
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,
CC         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|RuleBase:RU000554}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009935, ECO:0000256|RuleBase:RU004169}.
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:GBG00641.1}.
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DR   EMBL; BDRX01000275; GBG00641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0PRA2; -.
DR   STRING; 307507.A0A2V0PRA2; -.
DR   InParanoid; A0A2V0PRA2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-EC.
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   NCBIfam; TIGR01464; hemE; 1.
DR   PANTHER; PTHR21091; METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED; 1.
DR   PANTHER; PTHR21091:SF167; UROPORPHYRINOGEN DECARBOXYLASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01208; URO-D; 1.
DR   SUPFAM; SSF51726; UROD/MetE-like; 1.
DR   PROSITE; PS00906; UROD_1; 1.
DR   PROSITE; PS00907; UROD_2; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW   ECO:0000256|RuleBase:RU000554};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000554};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|RuleBase:RU000554};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498}.
FT   DOMAIN          63..72
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00906"
FT   DOMAIN          182..198
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00907"
SQ   SEQUENCE   405 AA;  43395 MW;  C94384CE305ECD22 CRC64;
     MHGTMRAAAA AQQQTAAAAA APRRAAPAGR ARAVRARAAA DAAASADPLL VRAARGEAVE
     RAPCWMMRQA GRYQAAYREL ARKHPSFRAR SETTELIVDI SLQPFRSFRP DGVILFSDIL
     TPLPALGVPF EIDDNKGPLI EHPIRSMEQL SQLHALDLSQ LTFVGDALGA LRSEVGGAAA
     VLGFVGSPWT LATYLVEGAS SSLYKTIKSM AQSQPALLEG MLGALAEGMA EYMCYQIEAG
     AQAIQVFDSW GGQLPPREWD RWSGPYLRRM IATVKARHPR VPLTLYANGS GGLLERMGAT
     GADVIGLDWT VDMADARRRL GAGQSVQGNV DPVVLFAERA AIEDAVVDCL TKAGPRGHIL
     NLGHGVLVGT PEDAVAHMFE LSKSIKYADL PNMQRPAQQQ RALVS
//
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