NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-98 / CGA009;
DOI=10.1038/nbt923; PubMed=14704707 [NCBI, ExPASy, EBI, Israel, Japan]
Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S.;
"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris.";
Nat. Biotechnol. 22:55-61(2004).

Comments

FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME) (By similarity).
CATALYTIC ACTIVITY: Magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + O₂ = 13¹-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADP⁺ + H₂O.
CATALYTIC ACTIVITY: 13¹-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + O₂ = 13¹-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADP⁺ + 2 H₂O.
CATALYTIC ACTIVITY: 13¹-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + O₂ = divinylprotochlorophyllide + NADP⁺ + 2 H₂O.
COFACTOR: Iron (By similarity).
PATHWAY: Porphyrin biosynthesis; bacteriochlorophyll biosynthesis (light-independent).
SIMILARITY: Belongs to the acsF 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

BX572597; CAE26993.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_946898.1; -.

3D structure databases

ModBase

Q6N9J7.

Enzyme and pathway databases

BioCyc

RPAL258594:RPA1552-MON; -.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0048529;	Molecular function: magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity (inferred from electronic annotation from HAMAP).
GO:0030494;	Biological process: bacteriochlorophyll biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0015979;	Biological process: photosynthesis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01840; -; 1.
PBIL [Tree]

InterPro

IPR008434; AcsF.
IPR003251; Rubrerythrin.
Graphical view of domain structure.

Pfam

PF02915; Rubrerythrin; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02029; AcsF; 1.

ProtoNet

Q6N9J7.

Genome annotation databases

GeneID

2691628; -.

GenomeReviews

BX571963_GR; RPA1552.

KEGG

rpa:RPA1552; -.

NMPDR

fig|258594.1.peg.1542; -.

Phylogenomic databases

HOGENOM

Q6N9J7; -.

Genome annotation databases

CMR

Q6N9J7; RPA1552.

Other

UniRef

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

Keywords

Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Complete proteome; Iron; Metal-binding; NADP; Oxidoreductase; Photosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 365`	`365`		`Aerobic magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase.`	`PRO_0000217534`

Sequence information

Length: 365 AA [This is the length of the unprocessed precursor]

Molecular weight: 42483 Da [This is the MW of the unprocessed precursor]

CRC64: 4D6E38C1AA35ED7B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIPMEGGAQG ALRTRPDIKG SVDSLNIAKQ DTILTPRFYT TDYAAMDKLD VSLVRAEWTA 

        70         80         90        100        110        120 
MMNELRADYN KSHFKKTDEF VNSDLDKLPP ELRAEFKDFL VSSLTAEFSG CVLYAEIKKR 

       130        140        150        160        170        180 
IKNPEIRELF GLLSRDEARH AGFINEILKD HGIGVDLSFL TKVKKYTYFR PKFIFYATYL 

       190        200        210        220        230        240 
SEKIGYARYI TIYRQMERHP ERRFHPIFKW FERWCNDEFR HGEAFALLMR ADPSLLSGVN 

       250        260        270        280        290        300 
KLWIRFFLLA VFSTMYVRDH MRPAFYEALG VDATDYGMQV FRITTEISKQ VFPVTINLDD 

       310        320        330        340        350        360 
PRFLQNLERL RIAAEKIDRS HSQGLLGKLK RPFYAASAAL AFGRLFLLPA KRNELPRVIG 


LRPAW

Q6N9J7 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