ID A0A1G9B280_9MICO Unreviewed; 385 AA.
AC A0A1G9B280;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|HAMAP-Rule:MF_00218};
DE Short=UPD {ECO:0000256|HAMAP-Rule:MF_00218};
DE Short=URO-D {ECO:0000256|HAMAP-Rule:MF_00218};
DE EC=4.1.1.37 {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|HAMAP-Rule:MF_00218};
GN Name=hemE {ECO:0000256|HAMAP-Rule:MF_00218};
GN ORFNames=SAMN05216282_10521 {ECO:0000313|EMBL:SDK33573.1};
OS Cryobacterium psychrotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=386301 {ECO:0000313|EMBL:SDK33573.1, ECO:0000313|Proteomes:UP000198701};
RN [1] {ECO:0000313|EMBL:SDK33573.1, ECO:0000313|Proteomes:UP000198701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5382 {ECO:0000313|EMBL:SDK33573.1,
RC ECO:0000313|Proteomes:UP000198701};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_00218,
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|HAMAP-Rule:MF_00218,
CC ECO:0000256|RuleBase:RU000554}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00218}.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009935, ECO:0000256|HAMAP-Rule:MF_00218,
CC ECO:0000256|RuleBase:RU004169}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|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; FNFU01000005; SDK33573.1; -; Genomic_DNA.
DR STRING; 386301.SAMN05216282_10521; -.
DR OrthoDB; 9806656at2; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000198701; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-UniRule.
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:SF169; UROPORPHYRINOGEN DECARBOXYLASE; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00218};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00218};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00218};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW Rule:MF_00218}; Reference proteome {ECO:0000313|Proteomes:UP000198701}.
FT BINDING 44..48
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT SITE 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ SEQUENCE 385 AA; 41084 MW; B7D57307F311A4F8 CRC64;
MFDRIEGVNL DAQHPLSSGQ TADSRLIRAY QGTRPDVTPV WFMRQAGRSL PEYRELRVGT
RMLDVCLDPE LASEITLQPV RRHGVDAGIF FSDIVVPLKL VGVDVEIVAG KGPVLGTATR
TAKDVAALTS LDPAILDDAL APISEAVART VAELGGTPLI GFAGAPFTLA AYLVEGGPSK
DHIHARTLMH ADPEAWAALM DWTAEVTGRF LRAQVLAGAS AAQLFDSWAG ALSREDYAAY
VAPASAQAIS HVRDLTYIER TPDAAADPTE IRRNVPVVHF GVGTGELLKE MHGIGADVVG
VDYRIPLDEA NRRLGGVVPI QGNVDPALLA APWPVLEAHL RDVLERGRLA PAHVLNLGHG
VPPETDPDVL TRIVGFVHEH SAASA
//