[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=7592416 [NCBI, ExPASy, EBI, Israel, Japan] Zeilstra-Ryalls J.H., Kaplan S.; "Aerobic and anaerobic regulation in Rhodobacter sphaeroides 2.4.1: the role of the fnrL gene."; J. Bacteriol. 177:6422-6431(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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.; "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."; Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX. Dedicated to bacteriochlorophyll biosynthesis (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 .
SUBCELLULAR LOCATION: Cytoplasm (Potential).
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

Z49746; CAA89819.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000143; ABA79875.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_353776.1; -.

3D structure databases

ModBase

P51008.

Enzyme and pathway databases

BioCyc

RSPH272943:RSP_0699-MON; -.

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

P51008.

Genome annotation databases

GeneID

3718177; -.

GenomeReviews

CP000143_GR; RHOS4_23070.

KEGG

rsp:RSP_0699; -.

NMPDR

fig|272943.3.peg.3048; -.

Phylogenomic databases

HOGENOM

P51008; -.

Genome annotation databases

CMR

P51008; RHOS4_23070.

Other

ProtoNet

P51008.

UniRef

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

Keywords

4Fe-4S; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; 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`	`1 450`	`450`	`Coproporphyrinogen III oxidase, anaerobic 2.`	`PRO_0000109950`
`REGION`	`112 113`	`2`	`S-adenosyl-L-methionine 2 binding (By similarity).`
`METAL`	`60 60`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`64 64`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`67 67`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`BINDING`	`54 54`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`66 66`		`S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity).`
`BINDING`	`111 111`		`S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`144 144`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`171 171`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`183 183`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`208 208`		`S-adenosyl-L-methionine 2 (By similarity).`

Sequence information

Length: 450 AA [This is the length of the unprocessed precursor]

Molecular weight: 49103 Da [This is the MW of the unprocessed precursor]

CRC64: CD391AB6F80BBA3E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVSHLAKL GLFDARVPRY TSYPTAPNFG VGVTENLHAD WISSIPAGGS ISLYLHVPFC 

        70         80         90        100        110        120 
RRLCWFCACR TQGTSSDAPV RAYAAALKSE LALLRARLAP GVRLARMHWG GGTPTLLPPT 

       130        140        150        160        170        180 
LIHELALAIR DAVPSDAETD FSVEIDPTEI DAARLDALFE AGMTRVSIGV QDFDPLIQQS 

       190        200        210        220        230        240 
IGREQSFELT QRLTEDLRHR GLMGLDADIL YGLPHQTAPG VADSVQKLLS LSPDRVAVLG 

       250        260        270        280        290        300 
YAHVPAVSRR QLMIPTASIP GPEERLDLFE TARTLILWDG YQQVGLDHFA RAGDPLAHAH 

       310        320        330        340        350        360 
ACGRLCRSFQ GYTDDRAEVL IGLGASAISR FPQGFTQNAP STSDHLRAIR SGRFSTARGH 

       370        380        390        400        410        420 
VLSDEDRLRG RMIEQLLCEF RISRAQILAR FAVAPERLET LFRTCAAAFP GVVEITGHGL 

       430        440        450 
EILEEGRPLA RIVARSFDRY DASGKPQGAI

P51008 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