ID A0A2T1EQG3_9CHRO Unreviewed; 508 AA.
AC A0A2T1EQG3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Light-independent protochlorophyllide reductase subunit B {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|HAMAP-Rule:MF_00353};
GN Name=chlB {ECO:0000256|HAMAP-Rule:MF_00353};
GN ORFNames=C7B70_01570 {ECO:0000313|EMBL:PSB34976.1};
OS Chlorogloea sp. CCALA 695.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Entophysalidaceae; Chlorogloea.
OX NCBI_TaxID=2107693 {ECO:0000313|EMBL:PSB34976.1, ECO:0000313|Proteomes:UP000238278};
RN [1] {ECO:0000313|EMBL:PSB34976.1, ECO:0000313|Proteomes:UP000238278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 695 {ECO:0000313|EMBL:PSB34976.1,
RC ECO:0000313|Proteomes:UP000238278};
RA Cohen D.B., Kent A.D.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB34976.1, ECO:0000313|Proteomes:UP000238278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 695 {ECO:0000313|EMBL:PSB34976.1,
RC ECO:0000313|Proteomes:UP000238278};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) 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|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|HAMAP-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; bacteriochlorophyll
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004800}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis (light-independent). {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|HAMAP-Rule:MF_00353}.
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000256|HAMAP-
CC Rule:MF_00353}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSB34976.1}.
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DR EMBL; PVWN01000002; PSB34976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1EQG3; -.
DR OrthoDB; 5717231at2; -.
DR UniPathway; UPA00669; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000238278; Unassembled WGS sequence.
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:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000238278}.
FT DOMAIN 12..426
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT DOMAIN 459..503
FT /note="Light-independent protochlorophyllide reductase
FT subunit B-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08369"
FT ACT_SITE 294
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 429..430
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00353"
SQ SEQUENCE 508 AA; 56901 MW; 4A3C2EBDDA310A22 CRC64;
MKLAYWMYAG PAHIGTLRVS SSFKNVHAIM HAPIGDDYFN VMRSMLERDR NFTPVTISSV
DRNVLARGSQ EKVVDNITRK DTEEHPDLIV LTPTCTSSIL QEDLENFVER ASIDTKCDVM
LADVNHYRVN ELQAADITLR QIVQLYTEKA RKKGELPTGK TEKPSVNIFG ISSLGFHNHH
DCTELKRLMT DLGIEINEVI PEAASVLNLK RLSQAWFNLV PYRELGVMSA KYLEQEFGMP
YVDITPMGVV ETARCIRKIQ QILNDQGADV NYEDFINEQT LYVSQAAWFS RSIDCQNLTG
KKAVVFGDST HAAAMTKILA REMGIHVVWA GTYCKYDAEW FKEQVGEYCD EVIITEDHGL
IGDAIARVEP SAIFGTQMER HVGKRLNIPC GVIAAPVHIQ NFPIGYKPFC GYEGTNQIAD
LVYNSFTLGM EDHLLEIFGG HDTKEVITKG ISAGSDLGWN KEAQAELNKV PGFVRGKVKR
NTEKFARDRG FSVISLEVMY AAKESVGA
//
