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Database: UniProt
Entry: X4ZPJ0_9BACL
LinkDB: X4ZPJ0_9BACL
Original site: X4ZPJ0_9BACL 
ID   X4ZPJ0_9BACL            Unreviewed;       288 AA.
AC   X4ZPJ0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   07-JUN-2017, entry version 16.
DE   RecName: Full=Nitrogenase {ECO:0000256|SAAS:SAAS00692419};
DE            EC=1.18.6.1 {ECO:0000256|SAAS:SAAS00692419};
GN   ORFNames=PSAB_21055 {ECO:0000313|EMBL:AHV99102.1};
OS   Paenibacillus sabinae T27.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV99102.1, ECO:0000313|Proteomes:UP000019772};
RN   [1] {ECO:0000313|EMBL:AHV99102.1, ECO:0000313|Proteomes:UP000019772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T27 {ECO:0000313|EMBL:AHV99102.1,
RC   ECO:0000313|Proteomes:UP000019772};
RX   PubMed=24651173;
RA   Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA   Chen X., Cheng Q., Chen S., Li J.;
RT   "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing
RT   Paenibacillus spp.: Organization, Evolution and Expression of the
RT   Nitrogen Fixation Genes.";
RL   PLoS Genet. 10:E1004231-E1004231(2014).
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; CP004078; AHV99102.1; -; Genomic_DNA.
DR   RefSeq; WP_025336564.1; NZ_CP004078.1.
DR   EnsemblBacteria; AHV99102; AHV99102; PSAB_21055.
DR   KEGG; psab:PSAB_21055; -.
DR   PATRIC; fig|1268072.3.peg.4339; -.
DR   KO; K02588; -.
DR   Proteomes; UP000019772; Chromosome.
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   Complete proteome {ECO:0000313|Proteomes:UP000019772};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019772}.
FT   MOD_RES     100    100       ADP-ribosylarginine; by dinitrogenase
FT                                reductase ADP-ribosyltransferase.
FT                                {ECO:0000256|PIRSR:PIRSR605977-50}.
SQ   SEQUENCE   288 AA;  30014 MW;  CD1A6F71EB7E47D9 CRC64;
     MAKRTKHIAI YGKGGIGKST TTSNISAALA EAGHRVIQIG CDPKSDSTNT LRGGDYLPTV
     IDSLRDSANV KLQDVSAVGF KGVLCIEAGG PVPGVGCAGR GINAAVGLLQ ELNVFEEYEA
     DYVLYDVLGD VVCGGFAVPI RDGITDRAYV VSSSDFMAIY AANNLFKAIG KYAPSGGARL
     GGIIGNSILP GYPESLITDF ASRTGASVAG FVPRSPVVAQ SELYGKTVIE ANPGSEQADV
     YRKLAAYVAE NENLSVPSPL NVTDLRDWAR SWGDAINQEA ASFSAAGR
//
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