[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1333567 [NCBI, ExPASy, EBI, Israel, Japan] Coomber S.A., Jones R.M., Jordan P.M., Hunter C.N.; "A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. I. Molecular cloning, transposon mutagenesis and sequence analysis of the gene."; Mol. Microbiol. 6:3159-3169(1992).
[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.
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.
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

S50573; AAB24393.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000143; ABA79493.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S28440; S28440.

RefSeq

YP_353394.1; -.

3D structure databases

ModBase

P33770.

Enzyme and pathway databases

BioCyc

RSPH272943:RSP_0317-MON; -.

Ontologies

GO:0051989;	Molecular function: coproporphyrinogen dehydrogenase activity (inferred from electronic annotation from EC).
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.

BLOCKS

P33770.

Genome annotation databases

GeneID

3719077; -.

GenomeReviews

CP000143_GR; RHOS4_19250.

KEGG

rsp:RSP_0317; -.

NMPDR

fig|272943.3.peg.1725; -.

Phylogenomic databases

HOGENOM

P33770; -.

Genome annotation databases

CMR

P33770; RHOS4_19250.

Other

ProtoNet

P33770.

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`	`1 452`	`452`	`Coproporphyrinogen III oxidase, anaerobic 1.`	`PRO_0000109948`
`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).`
`CONFLICT`	`195 197`		`ETL -> QSV (in Ref. 1; AAB24393).`
`CONFLICT`	`383 383`		`D -> E (in Ref. 1; AAB24393).`
`CONFLICT`	`400 409`		`PRIAEAAEKF -> LAHRRSGREV (in Ref. 1; AAB24393).`

Sequence information

Length: 452 AA [This is the length of the unprocessed precursor]

Molecular weight: 50054 Da [This is the MW of the unprocessed precursor]

CRC64: 36E1430A36C0D6C9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTNIALLQSL GLFDARVPRY TSYPAAPVFS GAVGADFQAQ AIEALDPAVP ISVYVHVPFC 

        70         80         90        100        110        120 
ERLCWFCACR TQGTQTLAPV EAYVGTLLQE LELVKQHLPA GVKAGRLHWG GGTPTILSPE 

       130        140        150        160        170        180 
LIHKLAQAIK AVIPFAEDYE FSVEIDPMMV DEPKIRALSE EGMNRASIGI QDFTDIVQNA 

       190        200        210        220        230        240 
IGREQPFENT KACVETLRRY GVHSLNTDLV YGLPHQNRES LAATIDKVLS LRPDRVAIFG 

       250        260        270        280        290        300 
YAHVPWMAKR QKLIDETVLP PDIERHELAN LAARLFTEGG FERIGIDHFA LPDDSMAVAA 

       310        320        330        340        350        360 
RSRKLRRNFQ GYTDDTCPTL LGIGASSISK FEQGYLQNTA ATAAYIKSIE EGRLPGYRGH 

       370        380        390        400        410        420 
RMTEEDYLHG RAIEMIMCDF FLDLPALRAR FGEPAETMVP RIAEAAEKFT PFVTVDADGS 

       430        440        450 
MSIAKEGRAL ARMIARLFDA YETPEARYSQ AS

P33770 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
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