|Function||magnesium-protoporphyrin IX monomethyl ester aerobic oxidative cyclase|
|Domain Trusted Cutoff||192.50|
|Domain Noise Cutoff||120.55|
|Mainrole Category||Biosynthesis of cofactors, prosthetic groups, and carriers|
|Subrole Category||Chlorophyll and bacteriochlorphyll|
|Gene Ontology Term||GO:0009975: cyclase activity molecular_function|
| ||GO:0015995: chlorophyll biosynthetic process biological_process|
|Entry Date||Oct 20 2003 11:58AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||This HMM respresents the oxidative cyclase responsible for forming the distinctive E-ring of the chlorin ring system under aerobic conditions . This enzyme is believed to utilize a binuclear iron center and molecular oxygen. There are two isoforms of this enzyme in some plants and cyanobacterai which are differentially regulated based on the levels of copper and oxygen [2,3]. This step is essential in the biosynthesis of both bacteriochlorophyll and chlorophyll under aerobic conditions (a separate enzyme, BchE, acts under anaerobic conditions). This enzyme is found in plants, cyanobacteria and other photosynthetic bacteria.|
RM PMID: 11790744
RT 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.
RA Pinta V, Picaud M, Reiss-Husson F, Astier C.
RL J Bacteriol. 2002 Feb;184(3):746-53.
RM PMID: 10811605
RT The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii.
RA Moseley J, Quinn J, Eriksson M, Merchant S.
RL EMBO J. 2000 May 15;19(10):2139-51.
RM PMID: 11910013
RT Reciprocal expression of two candidate di-iron enzymes affecting photosystem I and light-harvesting complex accumulation.
RA Moseley JL, Page MD, Alder NP, Eriksson M, Quinn J, Soto F, Theg SM, Hippler M, Merchant S.
RL Plant Cell. 2002 Mar;14(3):673-88.
DR HAMAP; MF_01840; 35 of 35|
|Genome Property||GenProp0144: chlorophyllide a biosynthesis from protoporphyrin IX (HMM)|
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