ID W6S2U9_9CLOT Unreviewed; 528 AA.
AC W6S2U9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Nitrogenase protein alpha chain {ECO:0000256|RuleBase:RU004022};
DE EC=1.18.6.1 {ECO:0000256|RuleBase:RU004022};
GN Name=nifD {ECO:0000313|EMBL:CDM70239.1};
GN ORFNames=CM240_3122 {ECO:0000313|EMBL:CDM70239.1};
OS Clostridium bornimense.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM70239.1, ECO:0000313|Proteomes:UP000019426};
RN [1] {ECO:0000313|EMBL:CDM70239.1, ECO:0000313|Proteomes:UP000019426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA Wibberg D., Puehler A., Schlueter A.;
RT "Complete genome sequence of Clostridum sp. M2/40.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU004022};
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}.
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DR EMBL; HG917869; CDM70239.1; -; Genomic_DNA.
DR RefSeq; WP_044040375.1; NZ_HG917869.1.
DR AlphaFoldDB; W6S2U9; -.
DR STRING; 1216932.CM240_3122; -.
DR KEGG; clt:CM240_3122; -.
DR PATRIC; fig|1216932.3.peg.3090; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_1_1_9; -.
DR OrthoDB; 9767044at2; -.
DR Proteomes; UP000019426; Chromosome 2.
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:UniProtKB-KW.
DR Gene3D; 3.40.50.12380; Nitrogenase MoFe cofactor biosynthesis protein NifE, C-terminal; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR010143; Nase_comp1_asu.
DR InterPro; IPR000318; Nase_comp1_CS.
DR NCBIfam; TIGR01862; N2-ase-Ialpha; 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.
DR PROSITE; PS00090; NITROGENASE_1_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU004022};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004022};
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 ECO:0000256|RuleBase:RU004022};
KW Reference proteome {ECO:0000313|Proteomes:UP000019426}.
FT DOMAIN 49..499
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT COILED 402..429
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 528 AA; 59258 MW; 83689D98E0240431 CRC64;
MSKVDSVLDK YSAKVYKNRK GHMLELEEET QEIAANSRTM PGLINHRGCC YAGCKGVVLG
PTKDALIITH GPIGCGFYSW GTRRNKAKAE DGGQNYVPYC FSTDLQESDI VFGGEKKLDA
AIEEAVNIFH PKTIFICATC PVGLIGDDLP AVAKRNSEKY GIDVISFPCE GYKGVSQSAG
HHIANNIIIR DLIGTVDYKP TKHSVNILGE YNIGGDAWEI KRILTLCGYE VIATFTGDGS
VDNYRKAHTA DLNVIQCHRS INYIAEMMKI QYGTAWMKGD FIGLDNTIET LREMAKFFDD
PVLIQQTEKV IADELANISD DMSLYRTKLR GKTAALFVGG SRSHHYQLLL KDFGVKTLLA
GYEFAHRDDY EGREVIPNIV EDADLKNIEV LNVEKIEDKY KVYKTEEELE ELKKEISELE
DYKGMERDMD KGSIVVDDLN HYETEEFIKK LKPDMFFSGI KDKFVIQKGG ILSRQLHSYD
YSGPYAGFKG AVNFGRDVTM GMYTPVWNYT VAPWKKESVL EGKLGGED
//