ID A0A2W7NE95_9BACT Unreviewed; 545 AA.
AC A0A2W7NE95;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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=LX69_01266 {ECO:0000313|EMBL:PZX17853.1};
OS Breznakibacter xylanolyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Breznakibacter.
OX NCBI_TaxID=990 {ECO:0000313|EMBL:PZX17853.1, ECO:0000313|Proteomes:UP000249239};
RN [1] {ECO:0000313|EMBL:PZX17853.1, ECO:0000313|Proteomes:UP000249239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6779 {ECO:0000313|EMBL:PZX17853.1,
RC ECO:0000313|Proteomes:UP000249239};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
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:PZX17853.1}.
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DR EMBL; QKZK01000008; PZX17853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7NE95; -.
DR OrthoDB; 9767044at2; -.
DR Proteomes; UP000249239; 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; 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 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:UP000249239}.
FT DOMAIN 59..520
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 545 AA; 61118 MW; C38740B2CEA17796 CRC64;
MGDKKKVDLT TFKDAVLDKY PKKVGKKRAK AIINNDPDNM PVIQANIRTI PGIITQRGCT
YAGCKGVVLG PTRDIVNITH GPIGCGFYSW LTRRNQTKTE SDQDANFIPY CFSTDMQDSN
IVFGGEEKLK QAIREARELF NPKAIAIFST CPVGLIGDDV HRVARQMKEE FNNEVNIFGF
SCEGYRGVSQ SAGHHIANNQ LYKNLIGNDD NVTPKSKFRV NLLGEYNIGG DAFEIERIFE
KCGVELVSTF SGNSTVSSFE QAHTADLTLV MCHRSINYVA EMLETSFGIP WFKVSFIGAQ
ASAKAMRKVA AYFNDPELTE RIEKVIAEEL KIVEAARQVA LPKTNGKTAM LFVGGSRAHH
YQDLFEELGV TTLSAGYEFG HRDDYEGRRV IPTIQIDADS RNIEEITVTK DEARFKERMT
PDVLKKMEDA LGKDEVEYND YNGLMAQIGK GALVIDDLSH YEMEKLIELY HPDIFCAGIK
EKYAVQKMGI PLKQLHNYDS GGPYAGFQGA MNFYNDIAMM VSTSIFKEIK APWEREEVVE
ASYVY
//
