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Database: UniProt
Entry: A0A3D9BWF8_9RHOB
LinkDB: A0A3D9BWF8_9RHOB
Original site: A0A3D9BWF8_9RHOB 
ID   A0A3D9BWF8_9RHOB        Unreviewed;       530 AA.
AC   A0A3D9BWF8;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   ORFNames=DRV84_06670 {ECO:0000313|EMBL:REC57847.1};
OS   Rhodosalinus sediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodosalinus.
OX   NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC57847.1, ECO:0000313|Proteomes:UP000257131};
RN   [1] {ECO:0000313|EMBL:REC57847.1, ECO:0000313|Proteomes:UP000257131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDN1C137 {ECO:0000313|EMBL:REC57847.1,
RC   ECO:0000313|Proteomes:UP000257131};
RX   PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA   Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT   "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT   saltern.";
RL   Int. J. Syst. Evol. Microbiol. 67:5108-5113(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 (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}.
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:REC57847.1}.
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DR   EMBL; QOHR01000005; REC57847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9BWF8; -.
DR   OrthoDB; 5717231at2; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000257131; 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: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:UP000257131}.
FT   DOMAIN          12..406
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   DOMAIN          481..525
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08369"
FT   REGION          428..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        274
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         409..410
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00353"
SQ   SEQUENCE   530 AA;  58316 MW;  D6D5A835CFC0C0AB CRC64;
     MKLSVWTYEG PPHVGAMRVA TGMTDLHYVL HAPQGDTYAD LLFTMIERRD HRPPVTYTTF
     QARDLGSDTA DLFKTACEDA YARFQPQAMI VGASCTAELI QDDPGGMAET MGMPIPIVPL
     ELPSYQRKEN FGCDETFFQL VKALARPVEK TEAITANLIG PTALGFRHRD DITEVTRHLE
     EMGVGVNVVG PMGATPEDLT RLGAAHFNVL MYPETAESAA RWMERELGLP FTKTVPIGVG
     ATRDFLEEVS GITGLPVRTD ESRLRLPWYS ASVDSTYLTG KRVFLFGDGT HVAAAARIAR
     DEMGFEVVGL GCYNREQARN IRRVAKDYGV EATITDDYLE VEAAIEAAAP EMILGTQMER
     HIGKRLGIPC AVISAPVHVQ DFPARYAPQM GFEGANVIFD TWVHPLVMGL EEHLLHMFRE
     DFEFHDEAGP SHHAAHAPAP RPAEPAHEGG AAPRPAAPDS PRDISTQEEG PAAAGGIEIV
     WRPAAEKELK KIPFFVRGKA KRNTEAFARE RGVAEIDVDT LYEAKAHYAR
//
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