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Database: UniProt
Entry: Q19V92
LinkDB: Q19V92
Original site: Q19V92 
ID   CHLB_CHLAT              Reviewed;         510 AA.
AC   Q19V92;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   15-MAR-2017, entry version 54.
DE   RecName: Full=Light-independent protochlorophyllide reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE            Short=DPOR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE            Short=LI-POR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE            EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00353};
GN   Name=chlB {ECO:0000255|HAMAP-Rule:MF_00353};
OS   Chlorokybus atmophyticus (Soil alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae;
OC   Chlorokybales; Chlorokybaceae; Chlorokybus.
OX   NCBI_TaxID=3144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.80;
RX   PubMed=17222354; DOI=10.1186/1741-7007-5-2;
RA   Lemieux C., Otis C., Turmel M.;
RT   "A clade uniting the green algae Mesostigma viride and Chlorokybus
RT   atmophyticus represents the deepest branch of the Streptophyta in
RT   chloroplast genome-based phylogenies.";
RL   BMC Biol. 5:2-2(2007).
CC   -!- FUNCTION: Component of the dark-operative protochlorophyllide
CC       reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce
CC       ring D of protochlorophyllide (Pchlide) to form chlorophyllide a
CC       (Chlide). This reaction is light-independent. The NB-protein
CC       (ChlN-ChlB) is the catalytic component of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- CATALYTIC ACTIVITY: Protochlorophyllide a + reduced ferredoxin + 2
CC       ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00353};
CC       Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is
CC       bound at the heterodimer interface by residues from both subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00353};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis (light-independent). {ECO:0000255|HAMAP-
CC       Rule:MF_00353}.
CC   -!- SUBUNIT: Protochlorophyllide reductase is composed of three
CC       subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB
CC       and two ChlN subunits. {ECO:0000255|HAMAP-Rule:MF_00353}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family.
CC       {ECO:0000255|HAMAP-Rule:MF_00353}.
DR   EMBL; DQ422812; ABD62177.2; -; Genomic_DNA.
DR   RefSeq; YP_001019110.1; NC_008822.1.
DR   ProteinModelPortal; Q19V92; -.
DR   SMR; Q19V92; -.
DR   GeneID; 4783226; -.
DR   UniPathway; UPA00670; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
DR   HAMAP; MF_00353; ChlB_BchB; 1.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR013580; P-CP/CP_red_C.
DR   InterPro; IPR005969; Protochl_reductB.
DR   InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   Pfam; PF08369; PCP_red; 1.
DR   PIRSF; PIRSF000163; PCP_ChlB; 1.
DR   TIGRFAMs; TIGR01278; DPOR_BchB; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Chloroplast; Iron;
KW   Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW   Photosynthesis; Plastid.
FT   CHAIN         1    510       Light-independent protochlorophyllide
FT                                reductase subunit B.
FT                                /FTId=PRO_0000324047.
FT   REGION      431    432       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00353}.
FT   ACT_SITE    296    296       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00353}.
FT   METAL        36     36       Iron-sulfur (4Fe-4S); shared with
FT                                heterodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00353}.
SQ   SEQUENCE   510 AA;  57474 MW;  37BA8884272F5630 CRC64;
     MKLAYWMYAG PAHIGTLRVA SSFKNVHAIM HAPLGDDYFN VMRSMLERER DFTPVTASIV
     DRHVLARGSQ NKVVENITRK DKEERPDLIV LTPTCTSSIL QEDLQNFVDR ASMDSESDVI
     LADVNHYRVN ELQAADRTLE QVVRFYIEKS KKQGDLNLTK TEKPSANILG IFTLGFHNQH
     DCRELKRLLQ ELGIEINEVI PEGGSVNNLK NLPRAWFNLV PYREVGLMTA IYLEKEFGMP
     YVSTTPMGVV DTATCIREIE KILNSFDKDV VVDFESYIDK QTRFVSQAAW FSRSIDCQNL
     TGKKAVVFGD ATHAASMTKI LAREMGINVA CAGTYCKHDA DWFKEQVQGY CDEVLITDDH
     TEVGDLIARI EPSAIFGTQM ERHIGKRLNI PCGVISAPVH IQNFPLGYRP FLGYEGTNQI
     ADLVYNSFTL GMEDHLLEIF GGHDTKEVIT KSLSTEEGLT WTSDAQAELS KIPGFVRGKI
     KRNTEKFARE NNISEINIEV MYAAKESLNA
//
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