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Entry: K8EFN2_9FIRM
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Original site: K8EFN2_9FIRM 
ID   K8EFN2_9FIRM            Unreviewed;       466 AA.
AC   K8EFN2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
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:CCO07501.1};
GN   ORFNames=DESHY_110445 {ECO:0000313|EMBL:CCO07501.1};
OS   Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO07501.1, ECO:0000313|Proteomes:UP000009315};
RN   [1] {ECO:0000313|EMBL:CCO07501.1, ECO:0000313|Proteomes:UP000009315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX   PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA   Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA   Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT   "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT   hydrothermale Lam5(T).";
RL   Genome Announc. 1:e00114-e00112(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCO07501.1}.
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DR   EMBL; CAOS01000003; CCO07501.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8EFN2; -.
DR   STRING; 1121428.DESHY_110445; -.
DR   eggNOG; COG2710; Bacteria.
DR   Proteomes; UP000009315; Unassembled WGS sequence.
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; 3.40.50.1980; 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   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; 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:CCO07501.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009315}.
FT   DOMAIN          26..449
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
SQ   SEQUENCE   466 AA;  51048 MW;  C1595F521316E3F7 CRC64;
     MLKMLDCTPK EIKERTGGAI NPAKTCQPIG AMYAALGIHK CLPHSHGSQG CCSYHRMHLT
     RHFRDPIMAS TSSFTEGASV FGGGANLKTA IKNVFAIYNP DIMAVHTTCL SETIGDDLPT
     IIRTAEIPEE KVVIHANTPS YQGSHVTGFS NMTKGMVNYL SEATLETKKN QANIIPGFVN
     PGDMREIKRI INTMGIKFIM FPDTSGVVDS PMTGEYVMYP RGGTRLADLK DTGNSKVTIA
     LGSYASADAA NQLERKCQVP AIVLKTPIGI KATDQLLMTL RSRFAVEIPY ELEEERGQLV
     DIMTDTHFHF HGKKVAIFGD PDIVLAITEF VLSLGMKPIY VLTGTPGTAG AIGSTLGNFE
     DDVRELLEEA NIEGRVKAGG DLFELHQWIK NEKVDLLIGN TYGKYIARAE DLPFVRLGFP
     ILDRSVHSHL PVVGYKGAIR LIEMISNALL DRADRDASDE DFELVM
//
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