[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Avonport; Reith M.E., Munholland J.; "Complete nucleotide sequence of the Porphyra purpurea chloroplast genome."; Plant Mol. Biol. Rep. 13:333-335(1995).

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; chlorophyll biosynthesis (light-independent).
SUBCELLULAR LOCATION: Plastid, chloroplast.
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

U38804; AAC08163.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S73198; S73198.

RefSeq

NP_053887.1; -.

3D structure databases

ModBase

P51277.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
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:0015995;	Biological process: chlorophyll biosynthetic process (inferred from electronic annotation from InterPro).
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.

Genome annotation databases

GeneID

809907; -.

Other

ProtoNet

P51277.

UniRef

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

Keywords

Chlorophyll biosynthesis; Chloroplast; Iron; Metal-binding; NADP; Oxidoreductase; Photosynthesis; Plastid.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 349`	`349`		`Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase.`	`PRO_0000217544`

Sequence information

Length: 349 AA [This is the length of the unprocessed precursor]

Molecular weight: 41550 Da [This is the MW of the unprocessed precursor]

CRC64: 2F46724F9D513D43 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQTTIQKEEA PNRETLLTPR FYTTDFEEMA SMNISENEQD FFAILEEFRA DYNSQHFIRG 

        70         80         90        100        110        120 
EEFNQSWSNL ETKTKSLFIE FLERSCTAEF SGFLLYKELS RKLKDSNPII AECFLLMSRD 

       130        140        150        160        170        180 
EARHAGFLNK AIGDFNLSLD LGFLTKTRKY TFFSPKFIFY ATYLSEKIGY WRYITIYRHM 

       190        200        210        220        230        240 
EQYPEHRIYP IFKFFENWCQ DENRHGDFFA ALLKSQPHFL NDWKAKMWCR FFLLSVFATM 

       250        260        270        280        290        300 
YLNDFQRIDF YNAIGLDSRQ YDMQVIRKTN ESAARVFPVA LDVDNPKFFK YLDSCACNNR 

       310        320        330        340 
ALIDIDKKGS QPLVKTFMKA PLYMSLILNL IKIYLIKPID SQAVWNTVR

P51277 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