ID C1DGZ8_AZOVD Unreviewed; 523 AA.
AC C1DGZ8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Nitrogenase molybdenum-iron protein beta chain {ECO:0000256|ARBA:ARBA00014775, ECO:0000256|RuleBase:RU364127};
DE EC=1.18.6.1 {ECO:0000256|ARBA:ARBA00012773, ECO:0000256|RuleBase:RU364127};
DE AltName: Full=Dinitrogenase {ECO:0000256|RuleBase:RU364127};
GN Name=nifK {ECO:0000313|EMBL:ACO76405.1};
GN OrderedLocusNames=Avin_01400 {ECO:0000313|EMBL:ACO76405.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO76405.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO76405.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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 ECO:0000256|RuleBase:RU364127}.
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:RU364127};
CC -!- COFACTOR:
CC Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143;
CC Evidence={ECO:0000256|RuleBase:RU364127};
CC Note=Binds 1 [8Fe-7S] cluster per heterodimer.
CC {ECO:0000256|RuleBase:RU364127};
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, ECO:0000256|RuleBase:RU364127}.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC {ECO:0000256|ARBA:ARBA00011002, ECO:0000256|RuleBase:RU004021}.
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DR EMBL; CP001157; ACO76405.1; -; Genomic_DNA.
DR RefSeq; WP_012698833.1; NC_012560.1.
DR AlphaFoldDB; C1DGZ8; -.
DR EMDB; EMD-26756; -.
DR EMDB; EMD-26757; -.
DR EMDB; EMD-26760; -.
DR EMDB; EMD-26763; -.
DR EMDB; EMD-26764; -.
DR EMDB; EMD-27639; -.
DR SMR; C1DGZ8; -.
DR STRING; 322710.Avin_01400; -.
DR EnsemblBacteria; ACO76405; ACO76405; Avin_01400.
DR KEGG; avn:Avin_01400; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_2_0_6; -.
DR OrthoDB; 9800746at2; -.
DR Proteomes; UP000002424; 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 CDD; cd01974; Nitrogenase_MoFe_beta; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR Gene3D; 1.20.89.10; Nitrogenase Molybdenum-iron Protein, subunit B, domain 4; 1.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR005976; Nase_Mo-Fe_CF_bsu.
DR InterPro; IPR024564; Nase_Mo-Fe_CF_bsu_N.
DR NCBIfam; TIGR01286; nifK; 1.
DR PANTHER; PTHR33712; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR PANTHER; PTHR33712:SF7; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR Pfam; PF11844; DUF3364; 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|RuleBase:RU364127};
KW Iron {ECO:0000256|RuleBase:RU364127};
KW Iron-sulfur {ECO:0000256|RuleBase:RU364127};
KW Metal-binding {ECO:0000256|RuleBase:RU364127};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231,
KW ECO:0000256|RuleBase:RU004021};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364127};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364127}.
FT DOMAIN 1..56
FT /note="Nitrogenase molybdenum-iron protein beta chain N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF11844"
FT DOMAIN 70..501
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 523 AA; 59460 MW; B6ECD633A24998F2 CRC64;
MSQQVDKIKA SYPLFLDQDY KDMLAKKRDG FEEKYPQDKI DEVFQWTTTK EYQELNFQRE
ALTVNPAKAC QPLGAVLCAL GFEKTMPYVH GSQGCVAYFR SYFNRHFREP VSCVSDSMTE
DAAVFGGQQN MKDGLQNCKA TYKPDMIAVS TTCMAEVIGD DLNAFINNSK KEGFIPDEFP
VPFAHTPSFV GSHVTGWDNM FEGIARYFTL KSMDDKVVGS NKKINIVPGF ETYLGNFRVI
KRMLSEMGVG YSLLSDPEEV LDTPADGQFR MYAGGTTQEE MKDAPNALNT VLLQPWHLEK
TKKFVEGTWK HEVPKLNIPM GLDWTDEFLM KVSEISGQPI PASLTKERGR LVDMMTDSHT
WLHGKRFALW GDPDFVMGLV KFLLELGCEP VHILCHNGNK RWKKAVDAIL AASPYGKNAT
VYIGKDLWHL RSLVFTDKPD FMIGNSYGKF IQRDTLHKGK EFEVPLIRIG FPIFDRHHLH
RSTTLGYEGA MQILTTLVNS ILERLDEETR GMQATDYNHD LVR
//
