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CHLN_SYNE7
ID   CHLN_SYNE7              Reviewed;         466 AA.
AC   P54208; Q31NB9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Light-independent protochlorophyllide reductase subunit N {ECO:0000255|HAMAP-Rule:MF_00352};
DE            Short=DPOR subunit N {ECO:0000255|HAMAP-Rule:MF_00352};
DE            Short=LI-POR subunit N {ECO:0000255|HAMAP-Rule:MF_00352};
DE            EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00352};
GN   Name=chlN {ECO:0000255|HAMAP-Rule:MF_00352}; Synonyms=frxC;
GN   OrderedLocusNames=Synpcc7942_1420;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7659748; DOI=10.1104/pp.108.4.1461;
RA   Ronen-Tarazi M., Lieman-Hurwitz J., Gabay C., Orus M.I., Kaplan A.;
RT   "The genomic region of rbcLS in Synechococcus sp. PCC 7942 contains genes
RT   involved in the ability to grow under low CO2 concentration and in
RT   chlorophyll biosynthesis.";
RL   Plant Physiol. 108:1461-1469(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the dark-operative protochlorophyllide reductase
CC       (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of
CC       protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This
CC       reaction is light-independent. The NB-protein (ChlN-ChlB) is the
CC       catalytic component of the complex. {ECO:0000255|HAMAP-Rule:MF_00352}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2
CC         phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-
CC         4S]-[ferredoxin]; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002,
CC         Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83348, ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00352};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00352};
CC       Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at
CC       the heterodimer interface by residues from both subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00352};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00352}.
CC   -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits;
CC       ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00352}.
CC   -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|HAMAP-
CC       Rule:MF_00352}.
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DR   EMBL; X67694; CAA47924.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57450.1; -; Genomic_DNA.
DR   RefSeq; WP_011378028.1; NC_007604.1.
DR   AlphaFoldDB; P54208; -.
DR   SMR; P54208; -.
DR   STRING; 1140.Synpcc7942_1420; -.
DR   PRIDE; P54208; -.
DR   EnsemblBacteria; ABB57450; ABB57450; Synpcc7942_1420.
DR   KEGG; syf:Synpcc7942_1420; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_037170_0_0_3; -.
DR   OMA; ISCVAWL; -.
DR   OrthoDB; 363662at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1420-MON; -.
DR   UniPathway; UPA00670; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
DR   GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
DR   HAMAP; MF_00352; ChlN_BchN; 1.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR005970; Protochl_reductN.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   PIRSF; PIRSF000162; P_chlorophyll_rd; 1.
DR   TIGRFAMs; TIGR01279; DPOR_bchN; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding; Oxidoreductase; Photosynthesis.
FT   CHAIN           1..466
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit N"
FT                   /id="PRO_0000208604"
FT   BINDING         23
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00352"
FT   BINDING         48
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00352"
FT   BINDING         108
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00352"
SQ   SEQUENCE   466 AA;  51540 MW;  9B1A51305045574C CRC64;
     MTTTEAPSAL SFECETGNYH TFCPISCVAW LYQKIEDSFF LVIGTKTCGY FLQNAMGVMI
     FAEPRYAMAE LEEGDISAQL NDYAELKRLC TQIKRDRNPS VIVWIGTCTT EIIKMDLEGL
     APKLEAEIGI PIVVARANGL DYAFTQGEDT VLAAMAARCP EAATSEADQQ ERTNAIQRLL
     QFGKSPAAEQ QPASSKHPPL ILFGSVPDPV ATQLTIELAK QGITVSGWLP AKRYTELPVI
     AEGSYAIGLN PFLSRTATTL MRRRKCKVIG APFPIGPDGS RAWIEKICSV LEIEPQGLAE
     REAQVWDSIE DYRQLVEGKQ VFFMGDNLWE ISLARFLVRC GMRCPEIGIP YLDRRYLGAE
     LAMLEATCQS MGVPLPRLVE KPDNYNQLQR IEALQPDLVI TGMAHANPLE ARGISTKWSV
     EFTFAQIHGF GNARAILELV TRPLRRNLAL GTLGGSQWVS EAVTSR
 
 
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