NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=S1;
PubMed=11790744 [NCBI, ExPASy, EBI, Israel, Japan]
Pinta V., Picaud M., Reiss-Husson F., Astier C.;
"Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester.";
J. Bacteriol. 184:746-753(2002).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=IL144;
Nagashima K.V., Igarashi N., Harada J., Nagashima S., Matsuura K., Shimada K.;
"Determination of nucleotide sequences of Rubrivivax gelatinosus Photosynthetic genes.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis in aerobic conditions. 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 .
MISCELLANEOUS: Bacteria lacking acsF do not exhibit a phenotype under photosynthesis or low-aeration respiratory growth conditions. In contrast, under highly aerated respiratory growth conditions, the absence of acsF leads to an accumulation of MgPMME.
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

AY234384; AAL25840.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB034704; BAA94050.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T50897; T50897.

3D structure databases

ModBase

Q8VPB5.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13266; -.

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.

TIGR02029; AcsF; 1.

Other

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 358`	`358`	`Aerobic magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase.`	`PRO_0000217533`
`CONFLICT`	`70 70`		`A -> P (in Ref. 2; BAA94050).`
`CONFLICT`	`128 128`		`N -> D (in Ref. 2; BAA94050).`
`CONFLICT`	`148 148`		`N -> D (in Ref. 2; BAA94050).`
`CONFLICT`	`229 231`		`SGA -> TGP (in Ref. 2; BAA94050).`
`CONFLICT`	`256 256`		`Q -> L (in Ref. 2; BAA94050).`
`CONFLICT`	`293 293`		`Q -> P (in Ref. 2; BAA94050).`
`CONFLICT`	`304 304`		`R -> H (in Ref. 2; BAA94050).`

Sequence information

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

Molecular weight: 41513 Da [This is the MW of the unprocessed precursor]

CRC64: 299E24EFFD4BFD9C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLATPTIESP EEAARRAKES TLLSPRFYTT DYAAMNAIDV SSIRAEWDAM LAEYEGDNNH 

        70         80         90        100        110        120 
DHFQRTPEFA QEVAERFSQV SPELRQEFLD FLVSSVTSEF SGCVLYNEIQ KNVENPDVKA 

       130        140        150        160        170        180 
LMRYMARNES RHAGFINQAL RDFGLGINLG GLKRTKAYTY FKPKYIFYAT YLSEKIGYAR 

       190        200        210        220        230        240 
YITIYRQLER HPDKRFHPIF RWFERWCNDE FRHGESFALI LRAHPHLISG ANLLWVRFFL 

       250        260        270        280        290        300 
LAVYATMYVR DHMRPQLHEA MGLESTDYDY RVFQITNEIS KQVFPISLDI DHQAFRAGME 

       310        320        330        340        350 
RLVRVKTKVD AAKARGGLVG RLQQAAWAAA GAATFARMYL IPVRRHALPA QVRMAPAW

Q8VPB5 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