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Database: UniProt
Entry: A0A074MBP5_ERYLO
LinkDB: A0A074MBP5_ERYLO
Original site: A0A074MBP5_ERYLO 
ID   A0A074MBP5_ERYLO        Unreviewed;       431 AA.
AC   A0A074MBP5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Light-independent protochlorophyllide reductase subunit N {ECO:0000256|HAMAP-Rule:MF_00352};
DE            Short=DPOR subunit N {ECO:0000256|HAMAP-Rule:MF_00352};
DE            Short=LI-POR subunit N {ECO:0000256|HAMAP-Rule:MF_00352};
DE            EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00352};
GN   Name=bchN {ECO:0000256|HAMAP-Rule:MF_00352};
GN   ORFNames=EH31_08665 {ECO:0000313|EMBL:KEO90155.1};
OS   Erythrobacter longus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO90155.1, ECO:0000313|Proteomes:UP000027647};
RN   [1] {ECO:0000313|EMBL:KEO90155.1, ECO:0000313|Proteomes:UP000027647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO90155.1,
RC   ECO:0000313|Proteomes:UP000027647};
RA   Zheng Q.;
RT   "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL   Submitted (APR-2014) 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_00352}.
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_00352};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00352};
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_00352};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC       biosynthesis (light-independent). {ECO:0000256|HAMAP-Rule:MF_00352}.
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_00352}.
CC   -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000256|HAMAP-
CC       Rule:MF_00352}.
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:KEO90155.1}.
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DR   EMBL; JMIW01000003; KEO90155.1; -; Genomic_DNA.
DR   RefSeq; WP_034959626.1; NZ_JMIW01000003.1.
DR   AlphaFoldDB; A0A074MBP5; -.
DR   STRING; 1044.EH31_08665; -.
DR   eggNOG; COG2710; Bacteria.
DR   OrthoDB; 5714774at2; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000027647; 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; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR   HAMAP; MF_00352; ChlN_BchN; 1.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR005970; Protochl_reductN.
DR   NCBIfam; TIGR01279; DPOR_bchN; 1.
DR   PANTHER; PTHR39429; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N; 1.
DR   PANTHER; PTHR39429:SF3; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   PIRSF; PIRSF000162; P_chlorophyll_rd; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00352};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Bacteriochlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Chlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00352};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027647}.
FT   DOMAIN          33..420
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   BINDING         33
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_00352"
FT   BINDING         58
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_00352"
FT   BINDING         119
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_00352"
SQ   SEQUENCE   431 AA;  47004 MW;  7D79981C963037BF CRC64;
     MSVATTLPGC DAPQAQSAAK PVLRERGQRE VFCGLTGIVW LHRKMQDAFF LVVGSRTCAH
     LLQSAAGVMI FAEPRFATAI MEERDLAGMV DAQDELDRVV TRLLERRPDI KTLFLVGSCP
     SEVIKLDLAK AAERLGAQYM PRVRILNYSG SGIETTFTQG EDACLAALVP VMPAEAEAAP
     KQLLMVGALP DIVEDQFLRL LGQLGIEHVG VLPARNARDL PPVGPNTRYI LAQPFLSDTA
     MALEGRGATR INALFPFGAE GTSDWLRAIG REFGIDSAHV EAVIAPGRER AARAIEHSKA
     ALQGKRVTFL PDSQLEVPLA RFLHTELGMD PVEVGTPYLH ASHCADEVAL LPETTRISEG
     QHVDNQLDRV RSDKPDLIVC GLGLANPLEA EGFTTKWAIE LVFSPIHGFD QAGDLAELFA
     RPMRRRDRLE V
//
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