P32920 (DCUP_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uroporphyrinogen decarboxylase
Short name=UPD
Short name=URO-D
EC=4.1.1.37

Gene names

Name:	hemE
Ordered Locus Names:	RHOS4_22880
ORF Names:	RSP_0680

Organism

Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)

Taxonomic identifier

272943 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. Ref.2
Catalytic activity	Uroporphyrinogen III = coproporphyrinogen + 4 CO2. HAMAP MF_00218
Enzyme regulation	Inhibited by N-ethyl-maleimide and phenylglyoxal. Ref.2
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. HAMAP MF_00218
Subunit structure	Homodimer By similarity. HAMAP MF_00218
Subcellular location	Cytoplasm Probable HAMAP MF_00218.
Sequence similarities	Belongs to the uroporphyrinogen decarboxylase family.
Biophysicochemical properties	Kinetic parameters: KM=1.8 µM for uroporphyrinogen I Ref.2 KM=6.0 µM for uroporphyrinogen III pH dependence: Optimum pH is 6.7-6.9.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Cellular component	Cytoplasm
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	uroporphyrinogen decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 343	343	Uroporphyrinogen decarboxylase HAMAP MF_00218		PRO_0000187632
Regions
	Region	23 – 27	5	Substrate binding By similarity
Sites
	Binding site	42	1	Substrate By similarity
	Binding site	73	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	205	1	Substrate By similarity
	Binding site	322	1	Substrate By similarity
	Site	73	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	18	1	P → S AA sequence Ref.2
	Sequence conflict	27	1	R → P AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P32920 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: 85E196904EB46BEF	FASTA	343	37,575
	10 20 30 40 50 60 MTKTMLRALK GETLPTPPIW LMRQAGRYLP EYRATRAQAG DFLSLCYTPD LAAEVTLQPI 70 80 90 100 110 120 RRYGFDAAIL FADILLLPQA LGADLWFETG EGPRMSTITD MAGVTALKGR DDIHETLAPV 130 140 150 160 170 180 YETCRILARE LPKETTFIGF AGMPWTVATY MIAGRGSKDQ AAAHKLKDTD RPAFEALMDR 190 200 210 220 230 240 VTEATIEYLA KQVEAGCEVV KLFDSWAGSL KGQDFEDFAV APAKRIVSEL KARFQGLPVI 250 260 270 280 290 300 AFPREAGEGY IGFAEKTGAD CVAIDNSVSP EWAAEKVQAG RTCVQGNLDP KYMVTGGEEL 310 320 330 340 VQATKRVVEA FRNGPHIFNL GHGITPEADP ENVTLLVETI RGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
[2]	"Purification and properties of the uroporphyrinogen decarboxylase from Rhodobacter sphaeroides." Jones R.M., Jordan P.M. Biochem. J. 293:703-712(1993) [PubMed: 8352737] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-30, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000143 Genomic DNA. Translation: ABA79856.1.
PIR	S35595.
RefSeq	YP_353757.1. NC_007493.1.
3D structure databases
ProteinModelPortal	P32920.
ModBase	Search...
Protein-protein interaction databases
STRING	P32920.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3718330.
GenomeReviews	Gene locus RHOS4_22880 in contig CP000143_GR.
KEGG	rsp:RSP_0680.
NMPDR	fig|272943.3.peg.2983.
PATRIC	23154523. VBIRhoSph57909_2632.
Phylogenomic databases
eggNOG	COG0407.
HOGENOM	HBG628392.
OMA	PRIHFGV.
PhylomeDB	P32920.
ProtClustDB	PRK00115.
Enzyme and pathway databases
BioCyc	RSPH272943:RSP_0680-MONOMER.
Family and domain databases
HAMAP	MF_00218. URO-D. [Tree]
InterPro	IPR006361. Uroporphyrinogen_deCO2ase_HemE. IPR000257. Uroporphyrinogen_deCOase. [Graphical view]
KO	K01599.
PANTHER	PTHR21091:SF2. HemE. 1 hit.
Pfam	PF01208. URO-D. 1 hit. [Graphical view]
TIGRFAMs	TIGR01464. HemE. 1 hit.
PROSITE	PS00906. UROD_1. 1 hit. PS00907. UROD_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCUP_RHOS4

Accession

Primary (citable) accession number: P32920
Secondary accession number(s): Q3J028

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program