NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LT2;
PubMed=8195073 [NCBI, ExPASy, EBI, Israel, Japan]
Xu K., Elliott T.;
"Cloning, DNA sequence, and complementation analysis of the Salmonella typhimurium hemN gene encoding a putative oxygen-independent coproporphyrinogen III oxidase.";
J. Bacteriol. 176:3196-3203(1994).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).

Comments

FUNCTION: Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX.
CATALYTIC ACTIVITY: Coproporphyrinogen-III + 2 S-adenosyl-L-methionine = protoporphyrinogen-IX + 2 CO₂ + 2 L-methionine + 2 5'-deoxyadenosine.
COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen III (AdoMet route): step 1/1 .
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the anaerobic coproporphyrinogen III oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U06779; AAA19690.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008887; AAL22843.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_462884.1; -.

3D structure databases

SMR

P0A1E1; 4-444.

ModBase

P0A1E1.

Enzyme and pathway databases

BioCyc

STYP99287:STM4004-MON; -.

Organism-specific databases

StyGene

SG10154; hemN.

Family and domain databases

InterPro

IPR006638; Elp3/MiaB/NifB.
IPR004558; HemN.
IPR010723; HemN_C.
IPR007197; Radical_SAM.
Graphical view of domain structure.

Pfam

PF06969; HemN_C; 1.
PF04055; Radical_SAM; 1.
Pfam graphical view of domain structure.

SMART

SM00729; Elp3; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00538; hemN; 1.

BLOCKS

P0A1E1.

Genome annotation databases

GeneID

1255530; -.

GenomeReviews

AE006468_GR; STM4004.

KEGG

stm:STM4004; -.

Phylogenomic databases

HOGENOM

P0A1E1; -.

Genome annotation databases

CMR

P0A1E1; STM4004.

Other

ProtoNet

P0A1E1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Porphyrin biosynthesis; S-adenosyl-L-methionine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 457`	`457`	`Oxygen-independent coproporphyrinogen III oxidase.`	`PRO_0000109952`
`REGION`	`113 114`	`2`	`S-adenosyl-L-methionine 2 binding (By similarity).`
`METAL`	`62 62`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`66 66`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`69 69`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`BINDING`	`56 56`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`68 68`		`S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity).`
`BINDING`	`112 112`		`S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`145 145`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`172 172`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`184 184`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`209 209`		`S-adenosyl-L-methionine 2 (By similarity).`

Sequence information

Length: 457 AA [This is the length of the unprocessed precursor]

Molecular weight: 52828 Da [This is the MW of the unprocessed precursor]

CRC64: 5667B4FE76204DAB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEQQIDWDL ALIQKYNYSG PRYTSYPTAL EFSEDFEDAA FLQAVARYPE RPLSLYVHIP 

        70         80         90        100        110        120 
FCHKLCYFCG CNKIVTRQQH KADQYLDALE QEIRHRAPLF ADRHVSQLHW GGGTPTYLNK 

       130        140        150        160        170        180 
AQISRLMTLL RENFHFNTDA EISIEVDPRE IELDVLDHLR AEGFNRLSMG VQDFNKEVQR 

       190        200        210        220        230        240 
LVNREQDEEF IFALLNHARD IGFTSTNIDL IYGLPKQTPE SFAFTLKRVT ELNPDRLSVF 

       250        260        270        280        290        300 
NYAHLPTLFA AQRKIKDADL PSAQQKLDIL QETIVSLTQA GYQFIGMDHF ARPDDELAVA 

       310        320        330        340        350        360 
QREGVLHRNF QGYTTQGDTD LLGMGVSAIS MIGDGYMQNQ KELKRYYQQV DERGNALWRG 

       370        380        390        400        410        420 
ITLTRDDCIR RDVIKALICN FRLDFNAVEQ QWGLHFAEYF AEDLQLLSPL AKDGLVDISE 

       430        440        450 
KGIQVTAKGR LLIRNICMCF DAYLRQKARM QQFSRVI

P0A1E1 in FASTA format

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View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools