NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/3.3.109; PubMed=8905231 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions.";
DNA Res. 3:109-136(1996).

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).
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

BA000022; BAA18220.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S75659; S75659.

RefSeq

NP_441540.1; -.

3D structure databases

ModBase

P74134.

Enzyme and pathway databases

BioCyc

SSP1148:SLL1874-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: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.

BLOCKS

P74134.

Genome annotation databases

GeneID

955012; -.

GenomeReviews

BA000022_GR; sll1874.

KEGG

syn:sll1874; -.

NMPDR

fig|1148.1.peg.1641; -.

Phylogenomic databases

HOGENOM

P74134; -.

Genome annotation databases

CMR

P74134; sll1874.

Other

ProtoNet

P74134.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 358`	`358`		`Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 2.`	`PRO_0000217540`

Sequence information

Length: 358 AA [This is the length of the unprocessed precursor]

Molecular weight: 41940 Da [This is the MW of the unprocessed precursor]

CRC64: 6B146529C9041EEA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVSTTLPTQL ETIRPGIKAP VKETLLTPRF YTTDFDKVAN LVLTLQDEEI EAALEELRAD 

        70         80         90        100        110        120 
YNRYHFVRND DFKRSFDHID GATRLAFIDF LERSCTSEFS GFLLFKELSR RLKNRSPKLA 

       130        140        150        160        170        180 
EAFHLLARDE ARHAGFINKA MADFGLSLDL RYLTQKRTYT FFPPEWVIYT VYLSEKIGYW 

       190        200        210        220        230        240 
RYILMFRHLE KNPDHNIYPL FNYFECWCQD ENRHGDFFKA LLRSQTALWK TWQSRLWSRF 

       250        260        270        280        290        300 
FLLTVFVTHT LTVFERTDFY QSVGLDAKQY NVDVVTNTNA TAARAFPEVL DTDNPKFFPR 

       310        320        330        340        350 
LEACASANEK LTAIANSEAP KLAKFCQKAP WIAVIIWQMI CIFLQKPVDA EARRGMVC

P74134 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