ID K6TXK1_9CLOT Unreviewed; 471 AA.
AC K6TXK1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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};
GN ORFNames=A370_04209 {ECO:0000313|EMBL:EKQ52376.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ52376.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ52376.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
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=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143;
CC Evidence={ECO:0000256|ARBA:ARBA00001919};
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC {ECO:0000256|RuleBase:RU004021}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ52376.1}.
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DR EMBL; ALXI01000139; EKQ52376.1; -; Genomic_DNA.
DR AlphaFoldDB; K6TXK1; -.
DR STRING; 1196322.A370_04209; -.
DR PATRIC; fig|1196322.3.peg.4106; -.
DR eggNOG; COG2710; Bacteria.
DR Proteomes; UP000001325; Unassembled WGS sequence.
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:0016163; F:nitrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051212; F:vanadium ion binding; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd01977; Nitrogenase_VFe_alpha; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR005974; Nase_asu.
DR InterPro; IPR010143; Nase_comp1_asu.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR010142; Nase_V-Fe_asu.
DR NCBIfam; TIGR01284; alt_nitrog_alph; 1.
DR NCBIfam; TIGR01862; N2-ase-Ialpha; 1.
DR NCBIfam; TIGR01860; VNFD; 1.
DR PANTHER; PTHR43457; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR PANTHER; PTHR43457:SF1; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR PROSITE; PS00699; NITROGENASE_1_1; 1.
PE 3: Inferred from homology;
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 Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231,
KW ECO:0000256|RuleBase:RU004021};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001325}.
FT DOMAIN 49..447
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 471 AA; 52691 MW; 6A06433C6B9E1AB1 CRC64;
MPLTLFKSDE LIPERKKHCY IKAPGEDITE FLPLSNIETI PGTLSERGCA FCGAKLVIGG
VLKDTIQMIH GPVGCAYDTW HTKRYPSDND NFQLKYVWST NMKESNVVFG GEKQLKASMI
EAFKQMPDIK RMFVYTTCAT ALIGDDPKAV AKQVMKELGD VDIFVVECPG FAGVSQSKGH
HVLNIGWINE KVGTVEPEIT SEYTVNLIGD YNIQGDAYVL HGYMEKLGIQ IIADFTGNAT
YDECRSMHRA QVSVVNCARS AGYLANELNK RYGIPRLDVD TWGFSYTAEA LRKVGVFFGI
EDKVEALIEE EMEKYKAKMD WYKERLSGKK VAIWTGGPRL WHWTKALEDD LGMTVVAMSS
KFGHQEDFEK VISRGHEGAI YIDDANELEF FDVLEMVHPD VVFTGPRVGD LIKKVHLPYV
NGHAYHNGPY MGFEGAVNMA RDIYNAVNSP MMKLAADDIV AQSKAIISES V
//
