Q8NT75 (DCUP_CORGL) 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:	Cgl0435, cg0516

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	358 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 By similarity. HAMAP MF_00218
Catalytic activity	Uroporphyrinogen III = coproporphyrinogen + 4 CO2. HAMAP MF_00218
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.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Cellular component	Cytoplasm
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome 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 – 358	358	Uroporphyrinogen decarboxylase HAMAP MF_00218		PRO_0000187600
Regions
	Region	36 – 40	5	Substrate binding By similarity
Sites
	Binding site	85	1	Substrate By similarity
	Binding site	160	1	Substrate By similarity
	Binding site	215	1	Substrate By similarity
	Binding site	338	1	Substrate By similarity
	Site	85	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NT75 [UniParc]. Last modified October 10, 2002. Version 1. Checksum: EF94F5E1789AE58F	FASTA	358	38,413
	10 20 30 40 50 60 MSALTIPAAR RTLNNAPIID AANGKTPTRT PVWFMRQAGR SLPEYKKVRE GISMLDSCFM 70 80 90 100 110 120 PELLAEITLQ PVRRHDVDAA ILFSDIVVPL RAAGVGVEIV AGRGPVLDAP VRSRGDVLNL 130 140 150 160 170 180 PILEGNVPEV EQGIGIILDE LSDSQALIGF AGAPFTLASY LVEGGPSKNH EKTKAMMHGD 190 200 210 220 230 240 PETWHALMAR LVPTIVNSLK SQIDAGIDAV QLFDSWAGFL TERDYTEFVL PYSTEILEEV 250 260 270 280 290 300 GKYQLPRIHF GVGTGELLGA MSKAGSEVMG VDWRVPLDKA AERIAAVSGP KVLQGNLDPA 310 320 330 340 350 LLFAGRAPLT KEIERIKAEA QTAVDAGHAT GHIFNLGHGV LPNTVAEDIT EAVSIIHS

References

[1]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB97828.1. BX927149 Genomic DNA. Translation: CAF19151.1.
RefSeq	NP_599682.1. NC_003450.3. YP_224737.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NT75.
ModBase	Search...
2D gel databases
World-2DPAGE	0001:Q8NT75.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1021107. 3344294.
GenomeReviews	Gene locus Cgl0435 in contig BA000036_GR. Gene locus cg0516 in contig BX927147_GR.
KEGG	cgb:cg0516. cgl:NCgl0420.
PATRIC	21492926. VBICorGlu203724_0434.
Phylogenomic databases
HOGENOM	HBG628392.
OMA	PRIHFGV.
PhylomeDB	Q8NT75.
ProtClustDB	PRK00115.
Enzyme and pathway databases
BioCyc	CGLU196627:CG0516-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_CORGL

Accession

Primary (citable) accession number: Q8NT75

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	October 10, 2002
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program