ID A0A318XG29_9FIRM Unreviewed; 530 AA.
AC A0A318XG29;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Nitrogenase protein alpha chain {ECO:0000256|RuleBase:RU004022};
DE EC=1.18.6.1 {ECO:0000256|RuleBase:RU004022};
GN ORFNames=LY28_03532 {ECO:0000313|EMBL:PYG84821.1};
OS Ruminiclostridium sufflavum DSM 19573.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=1121337 {ECO:0000313|EMBL:PYG84821.1, ECO:0000313|Proteomes:UP000248132};
RN [1] {ECO:0000313|EMBL:PYG84821.1, ECO:0000313|Proteomes:UP000248132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19573 {ECO:0000313|EMBL:PYG84821.1,
RC ECO:0000313|Proteomes:UP000248132};
RA Kyrpides N.;
RT "Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial
RT genomes (KMG-I) project.";
RL Submitted (JUN-2018) 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}.
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:PYG84821.1}.
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DR EMBL; QKMR01000030; PYG84821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318XG29; -.
DR OrthoDB; 9767044at2; -.
DR Proteomes; UP000248132; 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: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; 2.
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; 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 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:UP000248132}.
FT DOMAIN 51..501
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 530 AA; 59817 MW; 782F9AEBFBD353D8 CRC64;
MNVRNIVLDK YSAKVYKNRK EHIIEVNEET RQQPIAANTR SVPGIMTNRG CCYAGCKGVV
LGPLKDVLVL THGPIGCGFY SWGTRRNKAK PEDGRNFIEY CFSTDLQESD IVFGGEKKLR
QAIKEAVEIF NPKCIMICST CPVGLIGDDI HAVASDTERE YGISCMAFSC EGYKGVSQSG
GHHIANNTLI RKVIGTGDAE PTKRFTINML GEYNIGGDGW EVERLLKRIG YEIITVFTGD
GSYETMKNAH MANLNIVQCH RSINYIAEMM KTKYGVDWIK VNFIGLEAII QSLRDMATYF
GDNELTERTE AVILDELANI AEEKEYYYSK LKGKTAALYV GGSRSHHYQN LLADFGVKTV
LAGYEFAHRD DYEGREVIPT IKEDADSKNI EHLEVKKDER KFHAYLTEEQ YEELKTKIPL
EQYCGMIRTM EDNSVVVDDL NHFETEEFIK LLKPDMFFSG IKDKYVLQKS GVYSKQLHSY
DYSGPYAGFL GAINFARDLT MGLYTPAWGL VIPPWKNKST LKAKLAGGEK
//
