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Database: UniProt
Entry: BCHL_RHOCB
LinkDB: BCHL_RHOCB
Original site: BCHL_RHOCB 
ID   BCHL_RHOCB              Reviewed;         304 AA.
AC   D5ANS3; P26237;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   28-FEB-2018, entry version 45.
DE   RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein {ECO:0000255|HAMAP-Rule:MF_00355};
DE            Short=DPOR subunit L {ECO:0000255|HAMAP-Rule:MF_00355};
DE            Short=LI-POR subunit L {ECO:0000255|HAMAP-Rule:MF_00355};
DE            EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00355, ECO:0000269|PubMed:10811655};
GN   Name=bchL {ECO:0000255|HAMAP-Rule:MF_00355};
GN   OrderedLocusNames=RCAP_rcc00662;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RA   Burke D.H., Alberti M., Armstrong G.A., Hearst J.E.;
RL   Submitted (NOV-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/JB.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur
RT   bacterium Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=2203738; DOI=10.1128/jb.172.9.5001-5010.1990;
RA   Yang Z.M., Bauer C.E.;
RT   "Rhodobacter capsulatus genes involved in early steps of the
RT   bacteriochlorophyll biosynthetic pathway.";
RL   J. Bacteriol. 172:5001-5010(1990).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RC   STRAIN=SB1003 / CB1029;
RX   PubMed=10811655; DOI=10.1074/jbc.M002904200;
RA   Fujita Y., Bauer C.E.;
RT   "Reconstitution of light-independent protochlorophyllide reductase
RT   from purified bchL and bchN-bchB subunits. In vitro confirmation of
RT   nitrogenase-like features of a bacteriochlorophyll biosynthesis
RT   enzyme.";
RL   J. Biol. Chem. 275:23583-23588(2000).
RN   [5]
RP   CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=15953479; DOI=10.1016/j.bbabio.2005.02.002;
RA   Nomata J., Swem L.R., Bauer C.E., Fujita Y.;
RT   "Overexpression and characterization of dark-operative
RT   protochlorophyllide reductase from Rhodobacter capsulatus.";
RL   Biochim. Biophys. Acta 1708:229-237(2005).
RN   [6]
RP   CHARACTERIZATION, COFACTOR, AND IRON-SULFUR CLUSTER.
RX   PubMed=17064695; DOI=10.1016/j.febslet.2006.10.014;
RA   Nomata J., Kitashima M., Inoue K., Fujita Y.;
RT   "Nitrogenase Fe protein-like Fe-S cluster is conserved in L-protein
RT   (BchL) of dark-operative protochlorophyllide reductase from
RT   Rhodobacter capsulatus.";
RL   FEBS Lett. 580:6151-6154(2006).
CC   -!- FUNCTION: Component of the dark-operative protochlorophyllide
CC       reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce
CC       ring D of protochlorophyllide (Pchlide) to form chlorophyllide a
CC       (Chlide). This reaction is light-independent. The L component
CC       serves as a unique electron donor to the NB-component of the
CC       complex, and binds Mg-ATP. {ECO:0000269|PubMed:10811655}.
CC   -!- CATALYTIC ACTIVITY: Protochlorophyllide a + reduced ferredoxin + 2
CC       ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00355,
CC       ECO:0000269|PubMed:10811655, ECO:0000269|PubMed:15953479}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:17064695};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer.
CC       {ECO:0000269|PubMed:17064695};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism;
CC       bacteriochlorophyll biosynthesis (light-independent).
CC       {ECO:0000255|HAMAP-Rule:MF_00355}.
CC   -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of
CC       three subunits; BchL, BchN and BchB.
CC       {ECO:0000269|PubMed:15953479}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000255|HAMAP-Rule:MF_00355}.
DR   EMBL; Z11165; CAA77523.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE84427.1; -; Genomic_DNA.
DR   EMBL; M34843; AAA26098.1; -; Genomic_DNA.
DR   PIR; B36716; B36716.
DR   RefSeq; WP_013066406.1; NC_014034.1.
DR   ProteinModelPortal; D5ANS3; -.
DR   SMR; D5ANS3; -.
DR   STRING; 272942.RCAP_rcc00662; -.
DR   EnsemblBacteria; ADE84427; ADE84427; RCAP_rcc00662.
DR   GeneID; 31489608; -.
DR   KEGG; rcp:RCAP_rcc00662; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   KO; K04037; -.
DR   OMA; EVDFHHE; -.
DR   OrthoDB; POG091H0230; -.
DR   BioCyc; RCAP272942:G1GUE-666-MONOMER; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
DR   CDD; cd02032; Bchl_like; 1.
DR   HAMAP; MF_00355; ChlL_BchL; 1.
DR   InterPro; IPR030655; NifH/chlL_CS.
DR   InterPro; IPR000392; NifH/frxC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005971; Protochlorophyllide_ATP-bd.
DR   PANTHER; PTHR42864; PTHR42864; 1.
DR   PANTHER; PTHR42864:SF1; PTHR42864:SF1; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01281; DPOR_bchL; 1.
DR   PROSITE; PS00746; NIFH_FRXC_1; 1.
DR   PROSITE; PS00692; NIFH_FRXC_2; 1.
DR   PROSITE; PS51026; NIFH_FRXC_3; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
KW   Chlorophyll biosynthesis; Complete proteome; Iron; Iron-sulfur;
KW   Magnesium; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW   Photosynthesis; Reference proteome.
FT   CHAIN         1    304       Light-independent protochlorophyllide
FT                                reductase iron-sulfur ATP-binding
FT                                protein.
FT                                /FTId=PRO_0000409926.
FT   NP_BIND      46     51       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     216    217       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   NP_BIND     240    242       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
FT   METAL        50     50       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00355}.
FT   METAL       131    131       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000305}.
FT   METAL       165    165       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000305}.
FT   BINDING      75     75       ATP. {ECO:0000255|HAMAP-Rule:MF_00355}.
SQ   SEQUENCE   304 AA;  33205 MW;  3A49C39BCF15AECC CRC64;
     MSPRDDIPDL KGFDGDGEGS VQVHDSEDIG LDVGGARVFS VYGKGGIGKS TTSSNLSAAF
     SLLGKRVLQI GCDPKHDSTF TLTGRLQETV IDILKQVNFH PEELRPEDYV TEGFNGVMCV
     EAGGPPAGTG CGGYVVGQTV KLLKQHHLLE DTDVVVFDVL GDVVCGGFAA PLQHADRALI
     VTANDFDSIY AMNRIIAAVQ AKSVNYKVRL AGCVANRSRE TNEVDRYCEA ANFKRIAHMP
     DLDSIRRSRL KKRTLFEMDD AEDVVMARAE YIRLAETLWR STGEPGLTPE PLTDRHIFEL
     LGFD
//
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