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; BAA16583.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S74431; S74431.

RefSeq

NP_439903.1; -.

3D structure databases

ModBase

P72584.

Protein-protein interaction databases

IntAct

P72584; -.

Enzyme and pathway databases

BioCyc

SSP1148:SLL1214-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: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.

ProtoNet

P72584.

Genome annotation databases

GeneID

951877; -.

GenomeReviews

BA000022_GR; sll1214.

KEGG

syn:sll1214; -.

NMPDR

fig|1148.1.peg.4; -.

Phylogenomic databases

HOGENOM

P72584; -.

Genome annotation databases

CMR

P72584; sll1214.

Other

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 1.`	`PRO_0000217539`

Sequence information

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

Molecular weight: 42153 Da [This is the MW of the unprocessed precursor]

CRC64: 6E8BD879AB4767DC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVNTLEKPGF DEIRPGVKTP AKETILTPRF YTTDFDEMAK MDISPNEDEL RAILEEFRVD 

        70         80         90        100        110        120 
YNRHHFVRNE SFNKSWDHID GEKRQLFVEF LERSCTAEFS GFLLYKELGR RLKNKNPLLA 

       130        140        150        160        170        180 
ECFNLMSRDE ARHAGFLNKA MSDFNLSLDL GFLTKSRKYT FFKPKFIFYA TYLSEKIGYW 

       190        200        210        220        230        240 
RYITIYRHLE KNPNDCIYPI FEFFENWCQD ENRHGDFFDA IMRAQPHTLN DWKAKLWCRF 

       250        260        270        280        290        300 
FLLSVFATMY LNDTQRADFY ACLGLEARSY DKEVIEKTNE TAGRVFPIIL DVNNPEFYNR 

       310        320        330        340        350 
LETCVSNNEQ LRAIDASGAP GVIKALRKLP IFASNGWQFI KLYLMKPIAV DQLAGAVR

P72584 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