ID Q2L640_TAXDI Unreviewed; 513 AA.
AC Q2L640;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 72.
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:BAX56331.1};
OS Taxodium distichum (Bald cypress) (Cupressus disticha).
OG Plastid; Chloroplast {ECO:0000313|EMBL:BAE79295.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Taxodium.
OX NCBI_TaxID=28982 {ECO:0000313|EMBL:BAE79295.1};
RN [1] {ECO:0000313|EMBL:BAE79295.1}
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:BAX56331.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28039231; DOI=10.1093/gbe/evw278;
RA Wu C.-S., Chaw S.-M.;
RT "Large-Scale Comparative Analysis Reveals the Mechanisms Driving Plastomic
RT Compaction, Reduction, and Inversions in Conifers II (Cupressophytes).";
RL Genome Biol. Evol. 8:3740-3750(2016).
RN [3] {ECO:0000313|EMBL:BAX56331.1}
RP NUCLEOTIDE SEQUENCE.
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QGJ04652.1}
RP NUCLEOTIDE SEQUENCE.
RA Yang Y.;
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QYB22634.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=34282286;
RA Stull G.W., Qu X.J., Parins-Fukuchi C., Yang Y.Y., Yang J.B., Yang Z.Y.,
RA Hu Y., Ma H., Soltis P.S., Soltis D.E., Li D.Z., Smith S.A., Yi T.S.;
RT "Gene duplications and phylogenomic conflict underlie major pulses of
RT phenotypic evolution in gymnosperms.";
RL Nat. Plants 0:0-0(2021).
RN [6] {ECO:0000313|EMBL:QYB22634.1}
RP NUCLEOTIDE SEQUENCE.
RA Stull G., Qu X.-J., Parins-Fukuchi C., Yang Y.-Y., Yang J.-B., Yang Z.-Y.,
RA Hu Y., Ma H., Soltis P., Soltis D., Li D.-Z., Smith S., Yi T.-S.;
RL Submitted (JAN-2021) 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: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; AB232474; BAE79295.1; -; Genomic_DNA.
DR EMBL; LC177556; BAX56331.1; -; Genomic_DNA.
DR EMBL; MN535013; QGJ04652.1; -; Genomic_DNA.
DR EMBL; MW470995; QYB22634.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2L640; -.
DR BRENDA; 1.3.7.7; 12362.
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:BAE79295.1};
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:BAE79295.1}.
FT DOMAIN 12..430
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; 58362 MW; E88FC2EAA7F5A08C CRC64;
MKLAYWMYAG PAHIGTLRVA SSFKNVHAIM HAPLGDDYFN VMRSMLERER DFTAATASIV
DRHVLARGSQ ERVVDNILRK DKEEHPDLII LTPTCTSSIL QEDLQNFVNR ASIISDSDVI
FADVDHYQVN EIQAADRTLE QVVRYYLDRC HRQEKWDQFV TDAPSVNIIG IFTLGFHNQH
DCRELRRLLR DLDIEINQII PEGGSVEDLK NLPKAWFNLI PYREVGLMTA MYLNKEYGMP
YISTAPMGAV DMAEWIRQIQ KNVNTLALSS SSKRVDYEPY IDGQTRFVSQ AAWFSRSIDC
QNLTGKETVV FGDTTHAASI TKILVREMGI RVSCAGTYCK HDAEWFKEQI QGFCDEILIT
DDHAEVGDMI AHMEPSAIFG TQMERHIGKR LDIPCGVISA PVHIQNFPLG YRPFLGYEGT
NQIADLVYNS FALGMEDHLL DIFGGHDTKE IISKSLSTDI GLIWNPESRL ELSKIPRFAR
EKVERNTEKF ARQKGIETIT VEVMYAAKEA LNT
//
