ACSF2_SYNY3
ID ACSF2_SYNY3 Reviewed; 358 AA.
AC P74134;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 2 {ECO:0000255|HAMAP-Rule:MF_01840};
DE Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase 2 {ECO:0000255|HAMAP-Rule:MF_01840};
DE EC=1.14.13.81 {ECO:0000255|HAMAP-Rule:MF_01840};
GN Name=acsF2 {ECO:0000255|HAMAP-Rule:MF_01840}; OrderedLocusNames=sll1874;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA18220.1; -; Genomic_DNA.
DR PIR; S75659; S75659.
DR AlphaFoldDB; P74134; -.
DR IntAct; P74134; 2.
DR STRING; 1148.1653305; -.
DR PaxDb; P74134; -.
DR PRIDE; P74134; -.
DR EnsemblBacteria; BAA18220; BAA18220; BAA18220.
DR KEGG; syn:sll1874; -.
DR eggNOG; COG1633; Bacteria.
DR InParanoid; P74134; -.
DR OMA; ENRHGDC; -.
DR PhylomeDB; P74134; -.
DR BioCyc; MetaCyc:MON-17789; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000001425; 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; IBA:GO_Central.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IBA:GO_Central.
DR GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR CDD; cd01047; ACSF; 1.
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..358
FT /note="Magnesium-protoporphyrin IX monomethyl ester
FT [oxidative] cyclase 2"
FT /id="PRO_0000217540"
SQ SEQUENCE 358 AA; 41940 MW; 6B146529C9041EEA CRC64;
MVSTTLPTQL ETIRPGIKAP VKETLLTPRF YTTDFDKVAN LVLTLQDEEI EAALEELRAD
YNRYHFVRND DFKRSFDHID GATRLAFIDF LERSCTSEFS GFLLFKELSR RLKNRSPKLA
EAFHLLARDE ARHAGFINKA MADFGLSLDL RYLTQKRTYT FFPPEWVIYT VYLSEKIGYW
RYILMFRHLE KNPDHNIYPL FNYFECWCQD ENRHGDFFKA LLRSQTALWK TWQSRLWSRF
FLLTVFVTHT LTVFERTDFY QSVGLDAKQY NVDVVTNTNA TAARAFPEVL DTDNPKFFPR
LEACASANEK LTAIANSEAP KLAKFCQKAP WIAVIIWQMI CIFLQKPVDA EARRGMVC