DCUP_PSEAE
ID DCUP_PSEAE Reviewed; 355 AA.
AC P95458;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=PA5034;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-295.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Lu C.D., Kwon D.-H., Walthall D.A., Abdelal A.T.;
RT "Characterization of glutamate synthase from Pseudomonas aeruginosa PAO1.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AE004091; AAG08419.1; -; Genomic_DNA.
DR EMBL; U81261; AAB39261.1; -; Genomic_DNA.
DR PIR; F83017; F83017.
DR RefSeq; NP_253721.1; NC_002516.2.
DR RefSeq; WP_003114569.1; NZ_QZGE01000002.1.
DR PDB; 4WSH; X-ray; 1.95 A; A/B=1-355.
DR PDBsum; 4WSH; -.
DR AlphaFoldDB; P95458; -.
DR SMR; P95458; -.
DR STRING; 287.DR97_2389; -.
DR PaxDb; P95458; -.
DR PRIDE; P95458; -.
DR DNASU; 881202; -.
DR EnsemblBacteria; AAG08419; AAG08419; PA5034.
DR GeneID; 881202; -.
DR KEGG; pae:PA5034; -.
DR PATRIC; fig|208964.12.peg.5277; -.
DR PseudoCAP; PA5034; -.
DR HOGENOM; CLU_040933_0_0_6; -.
DR InParanoid; P95458; -.
DR OMA; LWLMRQA; -.
DR PhylomeDB; P95458; -.
DR BioCyc; PAER208964:G1FZ6-5150-MON; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000002438; 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:0019353; P:protoporphyrinogen IX biosynthetic process from glutamate; IBA:GO_Central.
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..355
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187626"
FT BINDING 27..31
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT SITE 78
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00218"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 176..200
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:4WSH"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:4WSH"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:4WSH"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:4WSH"
SQ SEQUENCE 355 AA; 38792 MW; 0776E76FD18DDEE6 CRC64;
MTALKNDRFL RALLKQPVDV TPVWMMRQAG RYLPEYRATR AKAGDFMSLC MNPELACEVT
LQPLDRYPQL DAAILFSDIL TIPDAMGQGL YFETGEGPRF RKVVSSLADI EALPVPDPEQ
DLGYVMDAVR TIRRELNGRV PLIGFSGSPW TLATYMVEGG SSKDFRKSKA MLYDNPKAMH
ALLDKLAQSV TSYLNGQIHA GAQAVQIFDS WGGSLSAAAY QEFSLAYMRK IVDGLIREHD
GRRVPVILFT KGGGLWLESM AEVGAEALGL DWTCDIGSAR ARVGERVALQ GNMDPSVLYA
NPAAIRAEVA RILAAYGKGT GHVFNLGHGI TPEVDPAHAG AFFEAVHELS AQYHG
