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Database: UniProt
Entry: Q2L631_CHALA
LinkDB: Q2L631_CHALA
Original site: Q2L631_CHALA 
ID   Q2L631_CHALA            Unreviewed;       513 AA.
AC   Q2L631;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Light-independent protochlorophyllide reductase subunit B {ECO:0000256|ARBA:ARBA00017673, ECO:0000256|HAMAP-Rule:MF_00353};
DE            Short=DPOR subunit B {ECO:0000256|HAMAP-Rule:MF_00353};
DE            Short=LI-POR subunit B {ECO:0000256|HAMAP-Rule:MF_00353};
DE            EC=1.3.7.7 {ECO:0000256|ARBA:ARBA00012713, ECO:0000256|HAMAP-Rule:MF_00353};
GN   Name=chlB {ECO:0000256|HAMAP-Rule:MF_00353,
GN   ECO:0000313|EMBL:AQM38961.1};
OS   Chamaecyparis lawsoniana (Lawson false cypress) (Cupressus lawsoniana).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:BAE79304.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC   Chamaecyparis.
OX   NCBI_TaxID=58030 {ECO:0000313|EMBL:BAE79304.1};
RN   [1] {ECO:0000313|EMBL:BAE79304.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16428257; DOI=10.1093/molbev/msj097;
RA   Kusumi J., Sato A., Tachida H.;
RT   "Relaxation of Functional Constraint on Light-Independent
RT   Protochlorophyllide Oxidoreductase in Thuja.";
RL   Mol. Biol. Evol. 23:941-948(2006).
RN   [2] {ECO:0000313|EMBL:AQM38961.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AQM38961.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28120880; DOI=10.1038/srep41005;
RA   Qu X.J., Jin J.J., Chaw S.M., Li D.Z., Yi T.S.;
RT   "Multiple measures could alleviate long-branch attraction in phylogenomic
RT   reconstruction of Cupressoideae (Cupressaceae).";
RL   Sci. Rep. 7:41005-41005(2017).
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:0000256|ARBA:ARBA00025201,
CC       ECO:0000256|HAMAP-Rule:MF_00353}.
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:0000256|ARBA:ARBA00000802, ECO:0000256|HAMAP-
CC         Rule:MF_00353};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00353};
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:0000256|HAMAP-Rule:MF_00353};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis (light-independent). {ECO:0000256|ARBA:ARBA00004949,
CC       ECO:0000256|HAMAP-Rule:MF_00353}.
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:0000256|ARBA:ARBA00025959, ECO:0000256|HAMAP-
CC       Rule:MF_00353}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_00353}.
CC   -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family.
CC       {ECO:0000256|ARBA:ARBA00008935, ECO:0000256|HAMAP-Rule:MF_00353}.
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DR   EMBL; KX832622; AQM38961.1; -; Genomic_DNA.
DR   EMBL; AB232480; BAE79304.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2L631; -.
DR   BRENDA; 1.3.7.7; 12361.
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-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   CDD; cd01981; Pchlide_reductase_B; 1.
DR   Gene3D; 1.20.89.20; -; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR   Gene3D; 1.10.8.550; Proto-chlorophyllide reductase 57 kD subunit B; 1.
DR   HAMAP; MF_00353; ChlB_BchB; 1.
DR   InterPro; IPR013580; LI-POR_suB-like_C.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR042298; P-CP_red_C.
DR   InterPro; IPR005969; Protochl_reductB.
DR   InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR   NCBIfam; TIGR01278; DPOR_BchB; 1.
DR   PANTHER; PTHR33712; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR   PANTHER; PTHR33712:SF7; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   Pfam; PF08369; PCP_red; 1.
DR   PIRSF; PIRSF000163; PCP_ChlB; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00353};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00353};
KW   Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171, ECO:0000256|HAMAP-
KW   Rule:MF_00353}; Chloroplast {ECO:0000313|EMBL:BAE79304.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00353};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00353};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00353};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00353};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00353};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_00353}; Plastid {ECO:0000313|EMBL:BAE79304.1}.
FT   DOMAIN          12..431
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   DOMAIN          464..508
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08369"
FT   ACT_SITE        299
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00353"
FT   BINDING         36
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00353"
FT   BINDING         434..435
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00353"
SQ   SEQUENCE   513 AA;  58462 MW;  24F0AE246202AF3C CRC64;
     MKLAYWMYAG PAHIGTLRVA SSFKNVHAIM HAPLGDDYFN VMRSMLERER DFTAATASIV
     DRHVLARGSQ ERVVDNILRK DQEEHPDLII LTPTCTSSIL QEDLHNFVNR ASIISHSDVI
     FADVDHYQVN EIQAADRTLE QVVRYYLDRC HRQEKWDQFL TDAPSVNIIG IFTLGFHNQH
     DCRELRRLLR DLDIEINQII PEGGSVEDLQ NLPKAWFNLI PYREVGLMTA VYLNKEYGMP
     YISIAPMGAV DMAEWIRQIQ KNVNTLTLSS SNKRVDYEPY IDGQTRFVSQ AAWFSRSIDC
     QNLTGKETVV FGDTTHAASI TKILVREMGI RVSCAGTYCK HDAEWFKEQI QGFCDEILIT
     DDHAEVGDMI ARMEPSAIFG TQMERHIGKR LDIPCGVISA PVHIQNFPLG YRPFLGYEGT
     NQIADLIYNS FALGMEDHLL DIFGGHDTKE IISKSLSTDI GLIWNPESRL ELNKIPRFAR
     EKVEINTEKF ARQKGIETIT VEVMYAAKEA LNT
//
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