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Database: UniProt
Entry: C4LAS7_TOLAT
LinkDB: C4LAS7_TOLAT
Original site: C4LAS7_TOLAT 
ID   C4LAS7_TOLAT            Unreviewed;       522 AA.
AC   C4LAS7;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
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   OrderedLocusNames=Tola_0652 {ECO:0000313|EMBL:ACQ92281.1};
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ92281.1, ECO:0000313|Proteomes:UP000009073};
RN   [1] {ECO:0000313|Proteomes:UP000009073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACQ92281.1, ECO:0000313|Proteomes:UP000009073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RX   PubMed=22180815; DOI=10.4056/sigs.2184986;
RA   Chertkov O., Copeland A., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA   Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J.,
RA   Brettin T., Larimer F., Land M., Hauser L., Spring S., Rohde M.,
RA   Kyrpides N.C., Ivanova N., Goker M., Beller H.R., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of Tolumonas auensis type strain (TA 4).";
RL   Stand. Genomic Sci. 5:112-120(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       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; CP001616; ACQ92281.1; -; Genomic_DNA.
DR   RefSeq; WP_012728880.1; NC_012691.1.
DR   AlphaFoldDB; C4LAS7; -.
DR   STRING; 595494.Tola_0652; -.
DR   KEGG; tau:Tola_0652; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_025876_2_0_6; -.
DR   OrthoDB; 9800746at2; -.
DR   Proteomes; UP000009073; 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:ACQ92281.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009073}.
FT   DOMAIN          1..56
FT                   /note="Nitrogenase molybdenum-iron protein beta chain N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11844"
FT   DOMAIN          70..500
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
SQ   SEQUENCE   522 AA;  58884 MW;  CE2CCE98D169F989 CRC64;
     MSQNIENIKS CYPLFEQDEY QNLFADKHAK YEEAHGDEKV REVFEWTTTQ EYKDLNFSRE
     ALTIDPAKAC QPLGAVLCSL GFEKTLPYVH GSQGCVAYFR TYFNRHFREP VACVSDSMTE
     DAAVFGGHAN MNDGLQNALA LYKPEMIAVS TTCMAEVIGD DLQAFTNNAK KDGFVPKDFP
     VPYAHTPSFV GSHITGWDNM FEGFCNTFTA DKADYKVGSN GKLNIVTGFE TYLGNYRVIK
     RMLTEMGVPF AMLSDPSEVL DTPSDGQYRM YAGGTTQDEM KDAPNAIDTL MLQPWHLVKT
     KKMVKETWGQ PATDLSIPMG LEWTDDFLMK VSALTGKAIP ASLELERGRL VDMITDSHTW
     LHGKKFGVYG DPDFVEGLVK FLLELGCEPN VILCNNGSKK WKKSMEKMLA DSPYGQGSEV
     YVGHDLWHFR SLMFTNKPDF MIGNSYGKFI QRDTLAKGKA FEVPLIRLGF PIFDRHHLHR
     MTTLGYEGAM YMLTTLVNAV MEKIDSETME LGKTDYNFDL VR
//
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