NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

Comments

FUNCTION: Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX (By similarity).
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 (By similarity).
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

AE000657; AAC07846.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B70482; B70482.

RefSeq

NP_214455.1; -.

3D structure databases

ModBase

O67886.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_2124-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051989;	Molecular function: coproporphyrinogen dehydrogenase activity (inferred from electronic annotation from EC).
GO:0004109;	Molecular function: coproporphyrinogen oxidase activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006779;	Biological process: porphyrin biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

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.

Genome annotation databases

GeneID

1193875; -.

GenomeReviews

AE000657_GR; aq_2124.

KEGG

aae:aq_2124; -.

NMPDR

fig|224324.1.peg.1470; -.

Phylogenomic databases

HOGENOM

O67886; -.

Genome annotation databases

CMR

O67886; aq_2124.

Other

ProtoNet

O67886.

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`	`1 456`	`456`	`Oxygen-independent coproporphyrinogen III oxidase.`	`PRO_0000109938`
`REGION`	`113 114`	`2`	`S-adenosyl-L-methionine 2 binding (By similarity).`
`METAL`	`61 61`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`65 65`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`68 68`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`BINDING`	`55 55`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`67 67`		`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: 456 AA [This is the length of the unprocessed precursor]

Molecular weight: 53785 Da [This is the MW of the unprocessed precursor]

CRC64: 4E494103B8EF6342 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAEFDKELI KKYDRPGPRY TSYPPATEFT EEVKEDEYVK RLIKSNERKT PLSLYFHIPF 

        70         80         90        100        110        120 
CEQRCLYCGC NVIISHRKGI EEPYLERVCR EMDLVSQYLD KDRKVIQLHW GGGTPNYLSP 

       130        140        150        160        170        180 
EQIKWFMEEI RKRFEFGDNA EISIELDPRY LTDEQIKAIK DAGFNRISLG VQDLDPKVQQ 

       190        200        210        220        230        240 
AVNRVQPYEL IKEKMEKLRE AGFESINLDL IYGLPYQTKE SFEKTVEKVI ELNPDRIATY 

       250        260        270        280        290        300 
SFAYIPQVKP HQQLLPKEAL PSAEEKLRIF EMVINKFQEA GYVYIGMDHF AKPEDELAVA 

       310        320        330        340        350        360 
QRKGELWRNF QGYTTKKGVE LLGFGATSIG MLYDSYFQNW KTLRDYNKTV DEGKIPVFRG 

       370        380        390        400        410        420 
YVLNEDDFIR REVIMDIMCN LGVEFSKIEN MFGINFREYF AKELEELKEM EEDGLIKVEE 

       430        440        450 
DRIKIMPVGR LLIRNVAMVF DAHLRRKKEL NFSRTI

O67886 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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