DCUP_AQUAE
ID DCUP_AQUAE Reviewed; 338 AA.
AC O66667;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000255|HAMAP-Rule:MF_00218};
DE Short=UPD {ECO:0000255|HAMAP-Rule:MF_00218};
DE Short=URO-D {ECO:0000255|HAMAP-Rule:MF_00218};
DE EC=4.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00218};
GN Name=hemE {ECO:0000255|HAMAP-Rule:MF_00218}; OrderedLocusNames=aq_334;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC uroporphyrinogen-III to yield coproporphyrinogen-III.
CC {ECO:0000255|HAMAP-Rule:MF_00218}.
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:0000255|HAMAP-Rule:MF_00218};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC {ECO:0000255|HAMAP-Rule:MF_00218}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00218}.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000255|HAMAP-Rule:MF_00218}.
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; AE000657; AAC06624.1; -; Genomic_DNA.
DR PIR; G70329; G70329.
DR RefSeq; NP_213227.1; NC_000918.1.
DR RefSeq; WP_010880165.1; NC_000918.1.
DR PDB; 2EJA; X-ray; 1.90 A; A/B=1-338.
DR PDBsum; 2EJA; -.
DR AlphaFoldDB; O66667; -.
DR SMR; O66667; -.
DR STRING; 224324.aq_334; -.
DR EnsemblBacteria; AAC06624; AAC06624; aq_334.
DR KEGG; aae:aq_334; -.
DR PATRIC; fig|224324.8.peg.267; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_0_0; -.
DR InParanoid; O66667; -.
DR OMA; LWLMRQA; -.
DR OrthoDB; 1104410at2; -.
DR UniPathway; UPA00251; UER00321.
DR EvolutionaryTrace; O66667; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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; Cytoplasm; Decarboxylase; Lyase; Porphyrin biosynthesis;
KW Reference proteome.
FT CHAIN 1..338
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187580"
FT BINDING 25..29
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT SITE 75
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2EJA"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 167..190
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:2EJA"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2EJA"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:2EJA"
SQ SEQUENCE 338 AA; 38687 MW; 92807A91AA2C8F9B CRC64;
MPKNDLLLRS LRGEPIGRFP VWLMRQAGRY MPEYRKIRNR VKNFLELCKN VDLATEISLL
PLKILGVDAI IIFSDILVPL EPLGVKVEFV EGEGPKLSWS GKVSDLKKYD PSQNAYVYEI
IKRVKEAQDE VPVIGFAGAP FTLLSYLIEG GASKDFKSTK LFMWENPKEY KRLMDILTET
VLAYLKEQIK AGADVVQIFD SWVNNLSLED YGEYVYPYVN YLISELKDFS DTPVIYFFRG
SSSFIDLAVD YRADALSVDW SVDIPELFKI YDKGFQGNLE PAVLYASEEV IEEKTLGLLR
RIPVKTRYVF NLGHGLAPDM ELEKVKYLVD LVKSFPLT
