ID Q60C79_METCA Unreviewed; 519 AA.
AC Q60C79;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
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:AAU90624.1};
GN OrderedLocusNames=MCA0231 {ECO:0000313|EMBL:AAU90624.1};
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU90624.1, ECO:0000313|Proteomes:UP000006821};
RN [1] {ECO:0000313|EMBL:AAU90624.1, ECO:0000313|Proteomes:UP000006821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath
RC {ECO:0000313|Proteomes:UP000006821};
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU90624.1; -; Genomic_DNA.
DR RefSeq; WP_010959596.1; NC_002977.6.
DR AlphaFoldDB; Q60C79; -.
DR STRING; 243233.MCA0231; -.
DR KEGG; mca:MCA0231; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_2_0_6; -.
DR Proteomes; UP000006821; 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,
KW ECO:0000313|EMBL:AAU90624.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006821}.
FT DOMAIN 1..56
FT /note="Nitrogenase molybdenum-iron protein beta chain N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF11844"
FT DOMAIN 70..495
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 519 AA; 58284 MW; F718D11CABD653A5 CRC64;
MSQNAEKVLD HFNLFREPEY INLFESKRKE FEFMPPDQQV EEVREWAKTE EYKEKNFARE
ALVVNPAKAC QPLGAVFAAV GFEGTIPFVH GSQGCVAYYR SHFSRHFKEP TSCVSSSMTE
DAAVFGGLNN MIDGLANTYN MYKPKMIAVS TTCMAEVIGD DLNAFIKTSK EKGSIPADFD
VPFAHTPAFV GSHITGYDNV MKGILQHFWD GKSGTVEPLV RQPNESINFL GGFDGYTVGN
LREIKRIFNL FGIDYTIIGD NSDVWDTPTD GEFRMYDGGT TLEQAANALH AKATISMQEF
CTEKTLPFIA EHGQEVVALN HPIGVKGTDR FLMEISRLTG KPIPVELEKE RGRLVDAIAD
STAHIHGQKF AIYGDPDLCY GLAEFLLELG AEPTHVLATN GGKAWETKMQ ALFDSSPFGK
NCKVYPGRDL WHMRSLLFTE PVDFLIGNTY GKYLERDTGT PLIRIGFPIF DRHHKHRYPV
WGYQGGLNVL VWILDRMFEA IDANTNIPAK TDYSFDIIR
//
