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Database: UniProt
Entry: Q6TFK2_9NOST
LinkDB: Q6TFK2_9NOST
Original site: Q6TFK2_9NOST 
ID   Q6TFK2_9NOST            Unreviewed;       210 AA.
AC   Q6TFK2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   13-SEP-2023, entry version 44.
DE   RecName: Full=nitrogenase {ECO:0000256|ARBA:ARBA00012773};
DE            EC=1.18.6.1 {ECO:0000256|ARBA:ARBA00012773};
DE   AltName: Full=Nitrogenase component I {ECO:0000256|ARBA:ARBA00030899};
DE   Flags: Fragment;
GN   Name=vnfDG {ECO:0000313|EMBL:AAQ99145.1};
OS   Anabaena azotica.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=197653 {ECO:0000313|EMBL:AAQ99145.1};
RN   [1] {ECO:0000313|EMBL:AAQ99145.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FACHB-118 {ECO:0000313|EMBL:AAQ99145.1};
RX   PubMed=16924483; DOI=10.1007/s00203-006-0150-4;
RA   Boison G., Steingen C., Stal L.J., Bothe H.;
RT   "The rice field cyanobacteria Anabaena azotica and Anabaena sp. CH1 express
RT   vanadium-dependent nitrogenase.";
RL   Arch. Microbiol. 186:367-376(2006).
CC   -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the iron
CC       protein (component 2) and a component 1 which is either a molybdenum-
CC       iron protein, a vanadium-iron, or an iron-iron protein.
CC       {ECO:0000256|ARBA:ARBA00004064}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16
CC         ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16
CC         phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997,
CC         ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=1.18.6.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000805};
CC   -!- COFACTOR:
CC       Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001915};
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
CC       {ECO:0000256|ARBA:ARBA00011515}.
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DR   EMBL; AY422692; AAQ99145.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6TFK2; -.
DR   BRENDA; 1.18.6.2; 15626.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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:InterPro.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 1.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR010143; Nase_comp1_asu.
DR   InterPro; IPR014279; Nase_V-Fe_dsu.
DR   InterPro; IPR004349; V/Nase_d_su.
DR   NCBIfam; TIGR02930; vnfG_nitrog; 1.
DR   PANTHER; PTHR43457; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   PANTHER; PTHR43457:SF1; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   Pfam; PF03139; AnfG_VnfG; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          8..75
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAQ99145.1"
FT   NON_TER         210
FT                   /evidence="ECO:0000313|EMBL:AAQ99145.1"
SQ   SEQUENCE   210 AA;  23729 MW;  C182A1486841A882 CRC64;
     ARGQEGTIYI DDGNELEFFE VLEMIRPDVV LTGPRVGALV KKLHLPYVNG HGYHNGPYMG
     FEGAVNMARD LYNAIYSPLM QLAAFDVRDD APKAPAKTKE IEHLNEKVTN ITTYIQERCL
     WQFHSRAWDR EENINGVIKK AAELLRGERS VQETLTGKLH YADAKILVSE LKRNLPWIKE
     LDKERVKSVL ESVKQNLVGI AISGSLNGEL
//
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