ACSF_PROMA
ID ACSF_PROMA Reviewed; 347 AA.
AC Q7VBV0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase {ECO:0000255|HAMAP-Rule:MF_01840};
DE Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase {ECO:0000255|HAMAP-Rule:MF_01840};
DE EC=1.14.13.81 {ECO:0000255|HAMAP-Rule:MF_01840};
GN Name=acsF {ECO:0000255|HAMAP-Rule:MF_01840}; OrderedLocusNames=Pro_0992;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
CC -!- FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll
CC biosynthesis. Mediates the cyclase reaction, which results in the
CC formation of divinylprotochlorophyllide (Pchlide) characteristic of all
CC chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester
CC (MgPMME). {ECO:0000255|HAMAP-Rule:MF_01840}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + Mg-protoporphyrin IX 13-monomethyl ester + 3 NADPH +
CC 3 O2 = 3,8-divinyl protochlorophyllide a + 5 H2O + 3 NADP(+);
CC Xref=Rhea:RHEA:33235, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58632, ChEBI:CHEBI:60491; EC=1.14.13.81;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01840};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01840};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_01840}.
CC -!- SIMILARITY: Belongs to the AcsF family. {ECO:0000255|HAMAP-
CC Rule:MF_01840}.
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DR EMBL; AE017126; AAQ00037.1; -; Genomic_DNA.
DR RefSeq; NP_875384.1; NC_005042.1.
DR RefSeq; WP_011125144.1; NC_005042.1.
DR AlphaFoldDB; Q7VBV0; -.
DR STRING; 167539.Pro_0992; -.
DR PRIDE; Q7VBV0; -.
DR EnsemblBacteria; AAQ00037; AAQ00037; Pro_0992.
DR GeneID; 54200335; -.
DR KEGG; pma:Pro_0992; -.
DR PATRIC; fig|167539.5.peg.1042; -.
DR eggNOG; COG1633; Bacteria.
DR HOGENOM; CLU_048037_0_0_3; -.
DR OMA; ENRHGDC; -.
DR OrthoDB; 366541at2; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000001420; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048529; F:magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01840; AcsF; 1.
DR InterPro; IPR008434; AcsF.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR003251; Rubrerythrin.
DR PANTHER; PTHR31053; PTHR31053; 1.
DR Pfam; PF02915; Rubrerythrin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR02029; AcsF; 1.
PE 3: Inferred from homology;
KW Chlorophyll biosynthesis; Iron; Metal-binding; NADP; Oxidoreductase;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..347
FT /note="Magnesium-protoporphyrin IX monomethyl ester
FT [oxidative] cyclase"
FT /id="PRO_0000217530"
SQ SEQUENCE 347 AA; 40465 MW; AAACDF2B53AAA97E CRC64;
MTTTTSGAPA SLGRNELPPH LDENLLTPRF YTTEFEKAAK TDLEIARKDF EAMFKEMEAD
YNLKHFDRKA SLERLDELSP EDKAVYESYL VRSVVSEFSG FLLFKEISNR FKKAGRQELG
QFFTFLARDE ARHAGFLGRA LKTEGINVDL PNLPKKRAAT FFPLSWVLYS LYLSEKIGYW
RYILINRHLK ANPDKVCAPL FDFFEPWCQD ENRHGDCINL MMRCWPGMTK GFRGKLLSRF
FLWTVFLTHT LTVCERGEFY ELLGIDPVLF DEEVIIQTNN TSKNAFPWVY KFEDGKFLSM
RIDILNAFKK WRNQNGIKKP LALGKFVLLI LKQFTLPMEK TDAVRYG