NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND INDUCTION.
DOI=10.1105/tpc.010420; PubMed=11910013 [NCBI, ExPASy, EBI, Israel, Japan]
Moseley J.L., Page M.D., Alder N.P., Eriksson M., Quinn J., Soto F., Theg S.M., Hippler M., Merchant S.;
"Reciprocal expression of two candidate di-iron enzymes affecting photosystem I and light-harvesting complex accumulation.";
Plant Cell 14:673-688(2002).

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).
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 metabolism; chlorophyll biosynthesis .
SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
INDUCTION: By Copper and oxygen.
SIMILARITY: Belongs to the acsF family.

Copyright

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Cross-references

Sequence databases

EMBL

AF337037; AAK32149.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF426027; AAL14712.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF337038; AAK32150.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_001691047.1; -.
XP_001691048.1; -.

UniGene

Cre.4405

3D structure databases

ModBase

Q9AR22.

Ontologies

GO:0048529;	Molecular function: magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

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

Pfam

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

TIGRFAMs

TIGR02029; AcsF; 1.

BLOCKS

Q9AR22.

Genome annotation databases

GeneID

5716556; -.

KEGG

cre:CHLREDRAFT_205856; -.

Other

ProtoNet

Q9AR22.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Chloroplast (Potential).`
`CHAIN`	`? 407`		`Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 2, chloroplastic.`	`PRO_0000000600`
`CONFLICT`	`18 18`		`P -> L (in Ref. 1; AAL14712).`
`CONFLICT`	`38 38`		`A -> V (in Ref. 1; AAL14712).`
`CONFLICT`	`356 356`		`N -> D (in Ref. 1; AAL14712).`

Sequence information

Length: 407 AA [This is the length of the unprocessed precursor]

Molecular weight: 47482 Da [This is the MW of the unprocessed precursor]

CRC64: 4C3A2920C158AA50 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATMLNKRVT GAFGKQAPVR SARVAAVRPS RSSVRVAATA APQEVEGFKV MRDGIKVASD 

        70         80         90        100        110        120 
ETLLTPRFYT TDFDEMERLF SLELNKNMDM EEFEAMLNEF KLDYNQRHFV RNETFKEAAE 

       130        140        150        160        170        180 
KIQGPTRKIF IEFLERSCTA EFSGFLLYKE LGRRLKATNP VVAEIFTLMS RDEARHAGFL 

       190        200        210        220        230        240 
NKAMSDFNLA LDLGFLTKNR KYTFFKPKFI FYATYLSEKI GYWRYISIYR HLQRNPDNQL 

       250        260        270        280        290        300 
YPLFEYFENW CQDENRHGDF FTAVLKARPE MVNDWAAKLW SRFFCLSVYI TMYLNDHQRD 

       310        320        330        340        350        360 
AFYSSLGLNT TQFNQHVIIE TNKSTERIFP AVPDVENPEF FRRMDLLVKY NAQLVNIGSM 

       370        380        390        400 
NLPSPIKAIM KAPILERMVA EVFQVFIMTP KESGSYDLDA NKTALVY

Q9AR22 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