ID F3YUU2_DESAF Unreviewed; 548 AA.
AC F3YUU2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Nitrogenase protein alpha chain {ECO:0000256|RuleBase:RU004022};
DE EC=1.18.6.1 {ECO:0000256|RuleBase:RU004022};
GN ORFNames=Desaf_0768 {ECO:0000313|EMBL:EGJ49119.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ49119.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ49119.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ49119.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
CC -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC complex that catalyzes the key enzymatic reactions in nitrogen
CC fixation. {ECO:0000256|ARBA:ARBA00002621}.
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=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409;
CC Evidence={ECO:0000256|ARBA:ARBA00001969};
CC -!- COFACTOR:
CC Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143;
CC Evidence={ECO:0000256|ARBA:ARBA00001919};
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC the iron protein (nitrogenase component 2).
CC {ECO:0000256|ARBA:ARBA00011462}.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC {ECO:0000256|RuleBase:RU004021}.
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DR EMBL; CP003221; EGJ49119.1; -; Genomic_DNA.
DR RefSeq; WP_014258953.1; NC_016629.1.
DR AlphaFoldDB; F3YUU2; -.
DR STRING; 690850.Desaf_0768; -.
DR KEGG; daf:Desaf_0768; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_1_1_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
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 InterPro; IPR005972; Nase_Mo-Fe_asu.
DR NCBIfam; TIGR01862; N2-ase-Ialpha; 1.
DR NCBIfam; TIGR01282; nifD; 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}; Molybdenum {ECO:0000256|ARBA:ARBA00022505};
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:UP000007844}.
FT DOMAIN 62..524
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 548 AA; 61657 MW; 43E1668D39CE6E34 CRC64;
MPTKKAMTPA EVKEEILKRY PTKVARKRDK QFLVHEGPEA MQTKDIQANV RTIPGIITQR
GCTYAGCKGV ILGPTRDIVN ITHGPIGCGF YSWLTRRNQT DASAPDAANY MTYCFSTDMT
EHDIVFGGMN KLRQAVQEAY DLFKPRAIAI FSTCPVGLIG DDVHAVAREM KEKLNAIDPN
HKVNIFAFSC EGYKGVSQSA GHHIANNQIF THVVGEEMKR PEGKYLINML GEYNIGGDAF
EIERILDKCG ITLNSSFSGN STYEQFARAG VADLNCVMCH RSINYVADMM ETKWGIPWIK
VNFIGAKSTA KSLRKIAQYF GDKQLIDRVE EVIAEEMKNV DATLADVKPR TTGKTAMLFV
GGSRAHHYQD LFKELGMRSI GAGYEFAHRD DYEGRRVIPD IKVDADSRNI EELHIEQDPA
NYNPRKTDEE LKQLEAAGFE FKEYAGLIPD MDKDTLIIDD INSWETEKLI EIMKPDIFCA
GIKEKYAVEK LGVPLKQLHN YDMGGPYAGF KGAVNYYLEI DRLVNSKIWS YLEAPWDKEP
ELSATYVG
//
