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Database: UniProt
Entry: D4J1L7_BUTFI
LinkDB: D4J1L7_BUTFI
Original site: D4J1L7_BUTFI 
ID   D4J1L7_BUTFI            Unreviewed;       291 AA.
AC   D4J1L7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   10-OCT-2018, entry version 39.
DE   RecName: Full=Nitrogenase {ECO:0000256|SAAS:SAAS00692419};
DE            EC=1.18.6.1 {ECO:0000256|SAAS:SAAS00692419};
GN   ORFNames=CIY_11690 {ECO:0000313|EMBL:CBK74006.1};
OS   Butyrivibrio fibrisolvens 16/4.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=657324 {ECO:0000313|EMBL:CBK74006.1};
RN   [1] {ECO:0000313|EMBL:CBK74006.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16/4 {ECO:0000313|EMBL:CBK74006.1};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Butyrivibrio fibrisolvens 16/4.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK74006.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16/4 {ECO:0000313|EMBL:CBK74006.1};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP
CC       + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16
CC       phosphate. {ECO:0000256|SAAS:SAAS00692418}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|SAAS:SAAS00700914};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS00700909}.
CC   -!- PTM: The reversible ADP-ribosylation of Arg inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity.
CC       {ECO:0000256|PIRSR:PIRSR605977-50}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700907}.
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DR   EMBL; FP929036; CBK74006.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4J1L7; -.
DR   STRING; 657324.CIY_11690; -.
DR   EnsemblBacteria; CBK74006; CBK74006; CIY_11690.
DR   KEGG; bfi:CIY_11690; -.
DR   PATRIC; fig|657324.3.peg.982; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   KO; K02588; -.
DR   BioCyc; BFIB657324:G131C-1013-MONOMER; -.
DR   GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
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:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   CDD; cd02040; NifH; 1.
DR   InterPro; IPR030655; NifH/chlL_CS.
DR   InterPro; IPR000392; NifH/frxC.
DR   InterPro; IPR005977; Nitrogenase_Fe_NifH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42864; PTHR42864; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR   SUPFAM; SSF52540; SSF52540; 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|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700918};
KW   ADP-ribosylation {ECO:0000256|PIRSR:PIRSR605977-50};
KW   ATP-binding {ECO:0000256|RuleBase:RU003688,
KW   ECO:0000256|SAAS:SAAS00700908};
KW   Iron {ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700910};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU003688,
KW   ECO:0000256|SAAS:SAAS00700920};
KW   Metal-binding {ECO:0000256|RuleBase:RU003688,
KW   ECO:0000256|SAAS:SAAS00700915};
KW   Nitrogen fixation {ECO:0000256|SAAS:SAAS00692421};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003688,
KW   ECO:0000256|SAAS:SAAS00700911};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003688,
KW   ECO:0000256|SAAS:SAAS00700919, ECO:0000313|EMBL:CBK74006.1}.
FT   MOD_RES     101    101       ADP-ribosylarginine; by dinitrogenase
FT                                reductase ADP-ribosyltransferase.
FT                                {ECO:0000256|PIRSR:PIRSR605977-50}.
SQ   SEQUENCE   291 AA;  30984 MW;  C69F5F79C2F8423F CRC64;
     MAEKIGKHIA IYGKGGIGKS TTTSNISAAL AEAGYRVIQI GCDPKSDSTN TLRGNNYLPT
     VLDSLREGNK IHLDDISVKG FGGVLCIESG GPVPGVGCAG RGINAAVNLL QELNLFEEFK
     PDYVLYDVLG DVVCGGFAVP IRDGITDRAY VVSSSDFMAL YAANNLFKAI NKYAPTGGAK
     LGGVIANSMK PGYHREIVDD FVAKTGTSIA GYVNRSLDVQ QSELYGKTVI EAKPNSAQAD
     IYRNLAKYIA ENENLVVPNP LGSAELRDWA RSWGDRIYDI ENGVVGVAEA I
//
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