NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/s002030050540; PubMed=9396835 [NCBI, ExPASy, EBI, Israel, Japan]
Lieb C., Siddiqui R.A., Hippler B., Jahn D., Friedrich B.;
"The Alcaligenes eutrophus hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase, is required for heme biosynthesis during anaerobic growth.";
Arch. Microbiol. 169:52-60(1998).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1244; PubMed=16964242 [NCBI, ExPASy, EBI, Israel, Japan]
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16.";
Nat. Biotechnol. 24:1257-1262(2006).

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 (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

U94742; AAB66374.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AM260479; CAJ94672.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_728040.1; -.

3D structure databases

ModBase

O34162.

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

O34162.

Genome annotation databases

GeneID

4247051; -.

GenomeReviews

AM260479_GR; H16_A3615.

KEGG

reh:H16_A3615; -.

Phylogenomic databases

HOGENOM

O34162; -.

Genome annotation databases

CMR

O34162; H16_A3615.

Other

ProtoNet

O34162.

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`	`1 494`	`494`	`Oxygen-independent coproporphyrinogen III oxidase.`	`PRO_0000109937`
`REGION`	`127 128`	`2`	`S-adenosyl-L-methionine 2 binding (By similarity).`
`METAL`	`75 75`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`79 79`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`82 82`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`BINDING`	`69 69`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`81 81`		`S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity).`
`BINDING`	`126 126`		`S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`159 159`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`186 186`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`198 198`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`223 223`		`S-adenosyl-L-methionine 2 (By similarity).`
`CONFLICT`	`63 65`		`Missing (in Ref. 1; AAB66374).`
`CONFLICT`	`480 481`		`QP -> HA (in Ref. 1; AAB66374).`

Sequence information

Length: 494 AA [This is the length of the unprocessed precursor]

Molecular weight: 54499 Da [This is the MW of the unprocessed precursor]

CRC64: CEDE1267B17A069F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIPSAITSPA PDRRALSDFR ALAGRIDGNG PRYTSYPTAD RFHNGPDLSL YHDALAACRA 

        70         80         90        100        110        120 
DAPAPLSLYL HIPFCENICY YCGCNKIITR DHGRSARYVN YLGREMALVA DRLGPRRQVL 

       130        140        150        160        170        180 
QSHWGGGTPT FLDPGEMRRV MALLHEHFEL AAEGEHSIEI DPRRVDHARM ALLAELGFNR 

       190        200        210        220        230        240 
VSLGVQDFDP EVQQAIHRIQ PFEETRAVVD AARTLGFRSV SLDLIYGLPH QTAARFGRTI 

       250        260        270        280        290        300 
DQVLALRPDR LSVYSYAHLP HVFKPQRRID ENALPPAGEK LDILVSTIER LSAEGYVYIG 

       310        320        330        340        350        360 
MDHFALPDDD LAVAQREGRL QRNFQGYSTH AGYDQVGLGI SAIGAIAGRY VQNARTLDEY 

       370        380        390        400        410        420 
YGALDHGRLP LARGVAMSAD DHLRREIIGA LMCNGVLDIP ALEARHGIRF GTAFAPELAD 

       430        440        450        460        470        480 
LAALGADGLV QCAPDRITVT PLGRLLVRRV AMVFDRYLRE DAARPASTGA QAVAANDGAQ 

       490 
PVRFVPRARY SRVV

O34162 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