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Database: UniProt
Entry: F0SYL1_SYNGF
LinkDB: F0SYL1_SYNGF
Original site: F0SYL1_SYNGF 
ID   F0SYL1_SYNGF            Unreviewed;       274 AA.
AC   F0SYL1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   28-MAR-2018, entry version 41.
DE   RecName: Full=Nitrogenase iron protein {ECO:0000256|HAMAP-Rule:MF_00533};
DE            EC=1.18.6.1 {ECO:0000256|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase Fe protein {ECO:0000256|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase component II {ECO:0000256|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase reductase {ECO:0000256|HAMAP-Rule:MF_00533};
GN   Name=nifH {ECO:0000256|HAMAP-Rule:MF_00533};
GN   OrderedLocusNames=Sgly_2853 {ECO:0000313|EMBL:ADY57123.1};
OS   Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Syntrophobotulus.
OX   NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY57123.1, ECO:0000313|Proteomes:UP000007488};
RN   [1] {ECO:0000313|Proteomes:UP000007488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the
CC       iron protein and the molybdenum-iron protein. {ECO:0000256|HAMAP-
CC       Rule:MF_00533}.
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|HAMAP-Rule:MF_00533,
CC       ECO:0000256|SAAS:SAAS00692418}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00533};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000256|HAMAP-
CC       Rule:MF_00533};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00533,
CC       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   -!- PTM: The reversible ADP-ribosylation of Arg-99 inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00533}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000256|HAMAP-Rule:MF_00533, ECO:0000256|RuleBase:RU003688,
CC       ECO:0000256|SAAS:SAAS00700907}.
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DR   EMBL; CP002547; ADY57123.1; -; Genomic_DNA.
DR   RefSeq; WP_013625943.1; NC_015172.1.
DR   STRING; 645991.Sgly_2853; -.
DR   EnsemblBacteria; ADY57123; ADY57123; Sgly_2853.
DR   KEGG; sgy:Sgly_2853; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   KO; K02588; -.
DR   OMA; EENEAYT; -.
DR   OrthoDB; POG091H0230; -.
DR   BioCyc; SGLY645991:G1GRR-2885-MONOMER; -.
DR   Proteomes; UP000007488; 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-UniRule.
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-UniRule.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR   CDD; cd02040; NifH; 1.
DR   HAMAP; MF_00533; 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   TIGRFAMs; TIGR01287; nifH; 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_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700918};
KW   ADP-ribosylation {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|PIRSR:PIRSR605977-50};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700908};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007488};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00533, ECO:0000256|RuleBase:RU003688,
KW   ECO:0000256|SAAS:SAAS00700910};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700920};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700915};
KW   Nitrogen fixation {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|SAAS:SAAS00692421};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700911};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700919,
KW   ECO:0000313|EMBL:ADY57123.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007488}.
FT   NP_BIND       8     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00533}.
FT   METAL        96     96       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   METAL       131    131       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   MOD_RES      99     99       ADP-ribosylarginine; by dinitrogenase
FT                                reductase ADP-ribosyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_00533,
FT                                ECO:0000256|PIRSR:PIRSR605977-50}.
SQ   SEQUENCE   274 AA;  30141 MW;  84DF5CEBB4B9CF5D CRC64;
     MRKIAIYGKG GIGKSTTQQN TAGAMAYFYD QKVFIHGCDP KADSTRLILG GMNQKTLMDV
     LRDEGEEKIT VDKVVKTGYK GIRCVESGGP EPGVGCAGRG VITAIDLMEK NGAYTPELDF
     VFFDVLGDVV CGGFAMPIRD GKAQEVYIVA SGEMMAIYAA NNICKGLLKY AKQSGVRLGG
     IICNSRKVDR EREFLEEFTS AIGTKLIHFM PRDNIVQKAE FNKKTVVEYD ADCNQAKEYG
     ELARKIIENK DFVIPQPLKM DELEAMVVKY GIAD
//
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