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Database: UniProt
Entry: A8L2C2_FRASN
LinkDB: A8L2C2_FRASN
Original site: A8L2C2_FRASN 
ID   A8L2C2_FRASN            Unreviewed;       518 AA.
AC   A8L2C2;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
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   ORFNames=Franean1_6879 {ECO:0000313|EMBL:ABW16213.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW16213.1};
RN   [1] {ECO:0000313|EMBL:ABW16213.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW16213.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA   Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT   "Complete sequence of Frankia sp. EAN1pec.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000820; ABW16213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8L2C2; -.
DR   STRING; 298653.Franean1_6879; -.
DR   KEGG; fre:Franean1_6879; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_025876_2_0_11; -.
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.
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:ABW16213.1}.
FT   DOMAIN          14..62
FT                   /note="Nitrogenase molybdenum-iron protein beta chain N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11844"
FT   DOMAIN          76..501
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
SQ   SEQUENCE   518 AA;  56945 MW;  19B41805B6958C11 CRC64;
     MTTTPETGSS IPLRVLDHSE LFKDEVYQKQ FEGKTEFENG SDSAEVARVL EWTRGWEYRE
     KNFAREALTV NPAKACQPLG AVLAGLGFQG TLPLVHGSQG CVAYFRSHFA RHFKEPVPAA
     STSMTEDAAV FGGLNNLVEA LENATSLYKP KMVAVSTTCM AEVIGEDLFA YIGAAKEKEV
     ISTDYPVPYA HTPSFVGSHI TGYDSMLKGI LENLTKSADA TEPKAGGKPR LNIIPGFETY
     TGNLREYRRV LELMGVDPLI LGDHADSLDS PADGEYDLYP GGTPLAEAAK AKFSRATVLL
     QESATRKTTE LIRDVWKQDT LVLETPIGVR GTDQFLTEIA RLAGVEIPAE LTVERGRLVD
     ALTDSHAYLH GKRVAIAGDP DLVVALTRFV LELGMIPVHV LSTNADTTFK ARMEKVLSAS
     KFGEAATVWP EKDLWHLRSL VFTEPVDLLI GSTYLKYISR EANVPLVRVG FPIFDRHHLH
     RFPIVGYTGG LHLLTQLVNT VLDELDRTSP DHSYDAVR
//
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