ID   ACSF_RUBGE              Reviewed;         358 AA.
AC   P0DJN9; Q8VPB5; Q9JPB1;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Aerobic magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase {ECO:0000255|HAMAP-Rule:MF_01840};
DE            Short=Aerobic 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};
OS   Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas
OS   gelatinosa).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX   NCBI_TaxID=28068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=S1;
RX   PubMed=11790744; DOI=10.1128/jb.184.3.746-753.2002;
RA   Pinta V., Picaud M., Reiss-Husson F., Astier C.;
RT   "Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved,
RT   putative binuclear-iron-cluster-containing protein involved in aerobic
RT   oxidative cyclization of Mg-protoporphyrin IX monomethylester.";
RL   J. Bacteriol. 184:746-753(2002).
CC   -!- FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll
CC       biosynthesis in aerobic conditions. Mediates the cyclase reaction,
CC       which results in the formation of divinylprotochlorophyllide (Pchlide)
CC       characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-
CC       monomethyl ester (MgPMME). {ECO:0000269|PubMed:11790744}.
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.
CC   -!- DISRUPTION PHENOTYPE: No phenotype under photosynthesis or low-aeration
CC       respiratory growth conditions. In contrast, under highly aerated
CC       respiratory growth conditions, the absence of AcsF leads to an
CC       accumulation of MgPMME. {ECO:0000269|PubMed:11790744}.
CC   -!- SIMILARITY: Belongs to the AcsF family. {ECO:0000255|HAMAP-
CC       Rule:MF_01840}.
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DR   EMBL; AY234384; AAL25840.2; -; Genomic_DNA.
DR   AlphaFoldDB; P0DJN9; -.
DR   SMR; P0DJN9; -.
DR   BioCyc; MetaCyc:MON-13266; -.
DR   BRENDA; 1.14.13.81; 5401.
DR   UniPathway; UPA00668; -.
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:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniRule.
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   Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Iron;
KW   Metal-binding; NADP; Oxidoreductase; Photosynthesis.
FT   CHAIN           1..358
FT                   /note="Aerobic magnesium-protoporphyrin IX monomethyl ester
FT                   [oxidative] cyclase"
FT                   /id="PRO_0000217533"
SQ   SEQUENCE   358 AA;  41513 MW;  299E24EFFD4BFD9C CRC64;
     MLATPTIESP EEAARRAKES TLLSPRFYTT DYAAMNAIDV SSIRAEWDAM LAEYEGDNNH
     DHFQRTPEFA QEVAERFSQV SPELRQEFLD FLVSSVTSEF SGCVLYNEIQ KNVENPDVKA
     LMRYMARNES RHAGFINQAL RDFGLGINLG GLKRTKAYTY FKPKYIFYAT YLSEKIGYAR
     YITIYRQLER HPDKRFHPIF RWFERWCNDE FRHGESFALI LRAHPHLISG ANLLWVRFFL
     LAVYATMYVR DHMRPQLHEA MGLESTDYDY RVFQITNEIS KQVFPISLDI DHQAFRAGME
     RLVRVKTKVD AAKARGGLVG RLQQAAWAAA GAATFARMYL IPVRRHALPA QVRMAPAW