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Database: UniProt
Entry: A0A254QPN3_9RHOB
LinkDB: A0A254QPN3_9RHOB
Original site: A0A254QPN3_9RHOB 
ID   A0A254QPN3_9RHOB        Unreviewed;       512 AA.
AC   A0A254QPN3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=ATO1_14385 {ECO:0000313|EMBL:OWU78180.1};
OS   Phaeobacter sp. 22II1-1F12B.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU78180.1, ECO:0000313|Proteomes:UP000197279};
RN   [1] {ECO:0000313|EMBL:OWU78180.1, ECO:0000313|Proteomes:UP000197279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU78180.1,
RC   ECO:0000313|Proteomes:UP000197279};
RA   Lai Q., Li G., Shao Z.;
RT   "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL   Submitted (APR-2013) 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 (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:OWU78180.1}.
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DR   EMBL; AQQP01000008; OWU78180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A254QPN3; -.
DR   OrthoDB; 5717231at2; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000197279; 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:UP000197279}.
FT   DOMAIN          12..406
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   DOMAIN          463..507
FT                   /note="Light-independent protochlorophyllide reductase
FT                   subunit B-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08369"
FT   REGION          429..448
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   512 AA;  56459 MW;  B98F1ED1B4A04BB6 CRC64;
     MKLTVWTYEG PPHVGAMRVA TAMKGLHYVL HAPQGDTYAD LLFTMIERRN HRPPVTYTTF
     QARDLGADTA MLFKTACRDA YDRFRPQAMI VGASCTAELI QDDPGGMAEA MELPVPVIAL
     DLPSYQRKEN FGADEALFQI TRALARPVDR TERVSCNLIG PTALGFRHRD DVTELTRLLS
     DMGVDVNVVA PLEATPADIA RLGAAHFNVL MYPETGESAC RWMERELGLP FTRTVPIGVG
     ATRDFVAEVA ELTGLAPRLD TKRLRLPWYT ASVDSTYLTG KRVFIFGDGT YVVSAARIAR
     DEMGFEVVGM GCYNREQARA VRRVASDFGL SALITDDYLD VEAAIADLAP ELILGTQMER
     HIGKRLGIPC AVISAPVHVQ DFPARYSPQM GLEGANVIFD TWVHPLVMGL EEHLLHMFRD
     DFEFHDDAGA SHHGGPAVPR SKAAPDPTPA VVDGAADPGT VIWLAEAESE LRKVPFFVRG
     KARRNTEAFA HDRGQHEISV ETLYEAKAHY AR
//
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