ID E2IGZ2_PTEAA Unreviewed; 514 AA.
AC E2IGZ2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 ORFNames=PTAQ_Cp004 {ECO:0000313|EMBL:ADK47557.1};
OS Pteridium aquilinum subsp. aquilinum (Bracken fern).
OG Plastid; Chloroplast {ECO:0000313|EMBL:ADK47557.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Dennstaedtiineae;
OC Dennstaedtiaceae; Pteridium.
OX NCBI_TaxID=104588 {ECO:0000313|EMBL:ADK47557.1};
RN [1] {ECO:0000313|EMBL:ADK47557.1}
RP NUCLEOTIDE SEQUENCE.
RA Der J.P., Duffy A.M., Kusner M., Gu C., Overvoorde P., Wolf P.G.;
RT "Complete chloroplast genome sequence and high levels of RNA editing in the
RT fern Pteridium aquilinum determined by massively parallel pyrosequencing.";
RL Submitted (JUN-2010) 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; HM535629; ADK47557.1; -; Genomic_DNA.
DR RefSeq; YP_003795561.1; NC_014348.1.
DR AlphaFoldDB; E2IGZ2; -.
DR GeneID; 9481216; -.
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:ADK47557.1};
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:ADK47557.1}.
FT DOMAIN 12..431
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT DOMAIN 465..509
FT /note="Light-independent protochlorophyllide reductase
FT subunit B-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08369"
FT REGION 465..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 514 AA; 57393 MW; F4904D109D890B59 CRC64;
MKLAYWMYAG PAHIGTLRVA SSFRNVHAIM HAPLGDDHFN VMRSMLERER DFTPVTASVV
DRHVLARGSQ EKVINNISRK DEEQRPDLIV STPTCTSSIS QEDLQNFVDR ASLSSESDVI
LADVNYHRVN ELQAADRTLE QIIRHYLDRA RKQGTLDRSV TDVPSANIIG IFTSGFHNQH
DCRELKRLPG ESGVSVNQVI PEGASLKYLK DLPRAWFNAV PYREVGLMTA TFSEKEYGMP
YISITPMGIS NTADFIEQIG KLVNVWASVL SERKLNYRLY VENQTKFVSQ AAWFSKSIDC
QNLAGKEAAI SGDATHAASI TKILVREMGI RVGCAGTYCK HDAERFNEQV QGLCDEVIVT
EDHTEVGDTI ARIEPSAIFG TQMERHIGKR MDIPCGVISS PVHIQNSPPG YRPFLGYEGT
NQIADLIYNS FNLGMEDHSP DVFGGHDTKE ISTKSLSTDK RDINWTPEAE SEPNRIPGFV
RGRTKKNTEV SAKQNDIPEI TADVMYAAKE QLSP
//
