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ACSF_PROM0
ID   ACSF_PROM0              Reviewed;         390 AA.
AC   A3PD22;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=P9301_10241;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000576; ABO17647.1; -; Genomic_DNA.
DR   RefSeq; WP_011862989.1; NC_009091.1.
DR   AlphaFoldDB; A3PD22; -.
DR   STRING; 167546.P9301_10241; -.
DR   EnsemblBacteria; ABO17647; ABO17647; P9301_10241.
DR   KEGG; pmg:P9301_10241; -.
DR   eggNOG; COG1633; Bacteria.
DR   HOGENOM; CLU_048037_0_0_3; -.
DR   OMA; FHPIFKW; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000001430; 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; 2.
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..390
FT                   /note="Magnesium-protoporphyrin IX monomethyl ester
FT                   [oxidative] cyclase"
FT                   /id="PRO_1000070545"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  45600 MW;  6D736E73A1CADCFC CRC64;
     MSQSTIESTN KKEINKGKAP AKETILSPRF YTTDFEAMEN MDLSINEEEL EAICEEFRKD
     YNRHHFVRNS EFEGAAEKLD PETRELFVDF LEGSCTSEFS GFLLYKELSK RIKDKNPLLA
     ECFAHMARDE ARHAGFLNKS MSDFGLQLDL GFLTANKDYT YFPPRSIFYA TYLSEKIGYW
     RYIAIYRHLE KNPNSKIFPL FNYFENWCQD ENRHGDFFDA LMKAQPRTVK SLSQKITIGG
     STFTHPLFDY FHRFRYFLNN LPLTSKLWSR FFLLAVFATM YARDLGIKKD FYSSLGLDAR
     DYDQFVINKT NETAARVFPV VMDVNNKSFY GRLDKIVENN KILSDIASGT GNKVSKTFRK
     VPKYLSNGYQ LLRLYLLKPL DSKDYQPSIR
 
 
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