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
//