ID D5V0S0_ARCNC Unreviewed; 343 AA.
AC D5V0S0;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=Arnit_2230 {ECO:0000313|EMBL:ADG93882.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG93882.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG93882.1, ECO:0000313|Proteomes:UP000000939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC {ECO:0000313|Proteomes:UP000000939};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
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}.
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DR EMBL; CP001999; ADG93882.1; -; Genomic_DNA.
DR RefSeq; WP_013136027.1; NC_014166.1.
DR AlphaFoldDB; D5V0S0; -.
DR STRING; 572480.Arnit_2230; -.
DR KEGG; ant:Arnit_2230; -.
DR eggNOG; COG0407; Bacteria.
DR HOGENOM; CLU_040933_0_0_7; -.
DR OrthoDB; 9806656at2; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000000939; Chromosome.
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:UP000000939}.
FT DOMAIN 18..27
FT /note="Uroporphyrinogen decarboxylase (URO-D)"
FT /evidence="ECO:0000259|PROSITE:PS00906"
FT DOMAIN 139..155
FT /note="Uroporphyrinogen decarboxylase (URO-D)"
FT /evidence="ECO:0000259|PROSITE:PS00907"
FT BINDING 23..27
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT SITE 73
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ SEQUENCE 343 AA; 38705 MW; 6D8A76493A4C5AB1 CRC64;
MSKIFVDACF RKPTPYTPVW MMRQAGRYLP EYMKVRAQAG NFLNLCHNPK LAAEVTIQPL
DIVGVDAAIL FSDILVIPNE MGMHLEFIKG EGPIFKDPIK TEAEVDALLG GSEAADKLTY
VYETIKLLKQ QLPEDKALIG FTGAPWTLAT YMIEGQGTKT YNICKKMMYS NPELLHKILK
KVTEVVKLYM ENQIKAGADV VQIFDSWAAA IEPAKYDEFS WKYMVEIADY LKEKYPHIPI
IMFPKGVPAF LDKVYGNFDV FGVDWGTPMA LAKEKLGDKY VLQGNMEPCR LYSKEATTMC
VEALQNIMQG DGHIFNLGHG ILPDVPVENA IHFVKECQRV SKK
//
