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Entry: E3I2I5_RHOVT
LinkDB: E3I2I5_RHOVT
Original site: E3I2I5_RHOVT 
ID   E3I2I5_RHOVT            Unreviewed;       311 AA.
AC   E3I2I5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   28-MAR-2018, entry version 52.
DE   RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein {ECO:0000256|HAMAP-Rule:MF_00355};
DE            Short=DPOR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
DE            Short=LI-POR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
DE            EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00355};
GN   Name=bchL {ECO:0000256|HAMAP-Rule:MF_00355};
GN   OrderedLocusNames=Rvan_0995 {ECO:0000313|EMBL:ADP70269.1};
OS   Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 /
OS   LMG 4299).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Hyphomicrobiaceae; Rhodomicrobium.
OX   NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP70269.1, 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
RT   alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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:0000256|HAMAP-Rule:MF_00355}.
CC   -!- CATALYTIC ACTIVITY: Protochlorophyllide a + reduced ferredoxin + 2
CC       ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00355}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00355};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000256|HAMAP-
CC       Rule:MF_00355};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism;
CC       bacteriochlorophyll biosynthesis (light-independent).
CC       {ECO:0000256|HAMAP-Rule:MF_00355}.
CC   -!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of
CC       three subunits; BchL, BchN and BchB. {ECO:0000256|HAMAP-
CC       Rule:MF_00355}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000256|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688}.
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DR   EMBL; CP002292; ADP70269.1; -; Genomic_DNA.
DR   RefSeq; WP_013418673.1; NC_014664.1.
DR   ProteinModelPortal; E3I2I5; -.
DR   STRING; 648757.Rvan_0995; -.
DR   EnsemblBacteria; ADP70269; ADP70269; Rvan_0995.
DR   KEGG; rva:Rvan_0995; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   HOGENOM; HOG000228825; -.
DR   KO; K04037; -.
DR   OMA; EVDFHHE; -.
DR   OrthoDB; POG091H0230; -.
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   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   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000313|EMBL:ADP70269.1};
KW   Bacteriochlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Chlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001399};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00355,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000313|EMBL:ADP70269.1};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001399}.
FT   NP_BIND      55     60       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
FT   NP_BIND     225    226       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
FT   NP_BIND     249    251       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
FT   METAL        59     59       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00355}.
FT   METAL       140    140       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00355}.
FT   METAL       174    174       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00355}.
FT   BINDING      84     84       ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
SQ   SEQUENCE   311 AA;  34068 MW;  A467F878F410A48B CRC64;
     MSMYTRIPAQ PIPQYRAKGA AGQDEGDGDG SMQVHLDPNM KIGNAKVFAV YGKGGIGKST
     TSSNLSVAFS KLGKRVLQIG CDPKHDSTFT LTKCMIPTVI DVLETVNFHT EELRPEDYMF
     EGYNGVMCVE AGGPPAGTGC GGYVVGQTVK LMKEHHLLDE TDVVVFDVLG DVVCGGFAAP
     LQYAERALIV TANDFDSIFA MNRIVAAIQA KSKNYRVRLG GVIANRSRAT DEIDRFNAAI
     GLKRMAHVPD LDCIRVSRLK KKTLFEMDPS EDVERAQAEY LQLAKAMWDG SEPLEAKPMK
     DRDIFEFLGF N
//
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