NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1128/JB.183.4.1300-1311.2001; PubMed=11157943 [NCBI, ExPASy, EBI, Israel, Japan]
Fischer H.-M., Velasco L., Delgado M.J., Bedmar E.J., Schaeren S., Zingg D., Goettfert M., Hennecke H.;
"One of two hemN genes in Bradyrhizobium japonicum is functional during anaerobic growth and in symbiosis.";
J. Bacteriol. 183:1300-1311(2001).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

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

AJ002517; CAA05507.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000040; BAC52351.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_773726.1; -.

3D structure databases

ModBase

O31381.

Enzyme and pathway databases

BioCyc

BJAP224911:BLL7086-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

O31381.

Genome annotation databases

GeneID

1047805; -.

GenomeReviews

BA000040_GR; bll7086.

KEGG

bja:bll7086; -.

Phylogenomic databases

HOGENOM

O31381; -.

Genome annotation databases

CMR

O31381; bll7086.

Other

ProtoNet

O31381.

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`	`1 450`	`450`	`Oxygen-independent coproporphyrinogen III oxidase.`	`PRO_0000109940`
`REGION`	`109 110`	`2`	`S-adenosyl-L-methionine 2 binding (By similarity).`
`METAL`	`57 57`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`61 61`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`64 64`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`BINDING`	`51 51`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`63 63`		`S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity).`
`BINDING`	`108 108`		`S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`141 141`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`168 168`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`180 180`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`205 205`		`S-adenosyl-L-methionine 2 (By similarity).`
`CONFLICT`	`307 307`		`Q -> H (in Ref. 1; CAA05507).`

Sequence information

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

Molecular weight: 49327 Da [This is the MW of the unprocessed precursor]

CRC64: EEAC485931754EE9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRADLAVSYG EERLPRYTSY PTAPHFSPVI DAGTYARWLS ELPAGASASL YLHVPFCREM 

        70         80         90        100        110        120 
CWYCGCHTQI VRRDDLIAAY QRTLRSEIAL VAETIGRRIK VEHIHFGGGT PTIMAPEAFA 

       130        140        150        160        170        180 
ELMAAMRQAF FVLPSAEIAV EIDPRTLTAD MVEAMRLSGV NRASLGVQSF DPIVQRAINR 

       190        200        210        220        230        240 
IQSFEQTAAV VDMLRHAGIA GINFDLIYGL PHQTVASCLD TVRRSLLLAP DRFSVFGYAH 

       250        260        270        280        290        300 
VPDFKKHQRM INQGALPDGP ARHDQACAIA NALKEAGYVQ IGLDHFARPD DSMAVAFEER 

       310        320        330        340        350        360 
TLRRNFQGYT TDQGEVLLGF GASAIGHLPQ GYVQNEVQIG AYAQSIGASR LATAKGYGLT 

       370        380        390        400        410        420 
DDDRLRADII ERIMCEFSAD LGDICARHGA EPEAMLKSAS RLKPLISDGV VRLDGDRLAV 

       430        440        450 
ANDSRFLVRS VAAAFDAHLD PGKQLHSRAV

O31381 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