ID E3I2I7_RHOVT Unreviewed; 522 AA.
AC E3I2I7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=bchB {ECO:0000256|HAMAP-Rule:MF_00353};
GN OrderedLocusNames=Rvan_0997 {ECO:0000313|EMBL:ADP70271.1};
OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS 4299).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Rhodomicrobium.
OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP70271.1, ECO:0000313|Proteomes:UP000001399};
RN [1] {ECO:0000313|Proteomes:UP000001399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC {ECO:0000313|Proteomes:UP000001399};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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 (BchN-BchB) 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 (light-independent). {ECO:0000256|HAMAP-Rule:MF_00353}.
CC -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits;
CC BchL, BchN and BchB. Forms a heterotetramer of two BchB and two BchN
CC subunits. {ECO:0000256|HAMAP-Rule:MF_00353}.
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000256|HAMAP-
CC Rule:MF_00353}.
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DR EMBL; CP002292; ADP70271.1; -; Genomic_DNA.
DR RefSeq; WP_013418675.1; NC_014664.1.
DR AlphaFoldDB; E3I2I7; -.
DR STRING; 648757.Rvan_0997; -.
DR KEGG; rva:Rvan_0997; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025470_0_0_5; -.
DR OrthoDB; 5717231at2; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000001399; Chromosome.
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:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
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 Bacteriochlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023181,
KW ECO:0000256|HAMAP-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:UP000001399}.
FT DOMAIN 12..410
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT DOMAIN 473..517
FT /note="Light-independent protochlorophyllide reductase
FT subunit B-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08369"
FT ACT_SITE 278
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 413..414
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00353"
SQ SEQUENCE 522 AA; 57473 MW; 323889B235AE443F CRC64;
MQLTVWTYEG PPHIGAMRVA TAMTGVHYVL HAPQGDTYAD LLFTMIERRD KRPPVTYTTF
QARDLGTDTA ELFQSALADA YERFKPQAML VGSSCTAELI QDDPGGLADA LRLPVPVIPL
ELPAYQKKEN WGAAETFYRI VRTLASPRQG QERPKNERPL ANLLGPTALG FRHRDDIVEI
TRLLDSMGIG VNVVAPLGAS PADIQRIPDA DFNLVLYPEH ALSAAQWLER AFKQPYTKTV
PIGVNATRAF IAEVAQIAGV SADVPERTRL PWYSRSVDST YLTGKRVFIF GDATHALAAA
RVASKELGFQ VVGLGTYSRE FAREIRAAAA EYGVEPLITD DYLEVEAAVR DSNPELVLGT
QMERHIAKRL GIPCAVISAP VHVQDFPARY SPQMGFEGAN VLFDTWVHPL MMGLEEHLLR
MFREDFEFQE APSHLGAAPQ APKEAPAARE LAVAAPAEVA LADTPATPSA LVWLADAEAE
LRKIPFFVRG KAKRNTERYA AEKGISNITV ETLYDAKAHF SR
//
