Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase |
Protein Synonyms/Alias | Mg-protoporphyrin IX monomethyl ester oxidative cyclase |
Gene Name | acsF |
Gene Synonyms/Alias | SYNPCC7002_A1992 |
Created Date | 3-June-2014 |
Organism | Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
NCBI Taxa ID | 32049 |
Phosphorylation | Position | Peptide | Code | Type | References | 238 | TWQSRLWSRFFLLTV | S | HTP | [1] | |
Reference | [1]Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002. Yang MK,Qiao ZX,Zhang WY,Xiong Q,Zhang J,Li T,Ge F,Zhao JD J. Proteome Res. 2013, Apr, 5;12(4):1909-23. [ PMID:23461524] |
Functional Description From UniProt | 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) |
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| Chlorophyllbiosynthesis; Completeproteome; Iron; Metal-binding; NADP; Oxidoreductase; Photosynthesis |
Protein Sequence | MVTLTDQPSP ELLRPGVKKP VQETLLTPRF YTTDFDKIAN MVLSSHEEEI LAALEELRAD 60 YNRNHFIRDE SFEQSWDHFD EKTRSIFIDF LERSCTSEFS GFLLFKELSR RLRDRSPILA 120 EAFHLLARDE ARHAGFINKS MVDFGLCLDL KYLTQKRTYT FFPPEWVIYT VYLSEKIGYW 180 RYILVYRHLE KHPEHNIYPL FKYFESWCQD ENRHGDFFKA LLRSQKSLWK TWQSRLWSRF 240 FLLTVFVTHS LTTLERSDFY EMIGLDAHQY NRDVIRNTNE TSLRAFPEVL DTNHPQFFTR 300 LEACAAANEH LKAIATNGNP KVIQFFQKIP WIINIVWHMA LIFFTKPVDA EALRAEVH 358 |
| GO:0005506 F:iron ion binding IEA:UniProtKB-HAMAP GO:0048529 F:magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity IEA:UniProtKB-HAMAP GO:0036068 P:light-independent chlorophyll biosynthetic process IEA:UniProtKB-UniPathway GO:0015979 P:photosynthesis IEA:UniProtKB-HAMAP |
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