ID D4H6V8_DENA2 Unreviewed; 503 AA.
AC D4H6V8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=Dacet_1048 {ECO:0000313|EMBL:ADD67824.1};
OS Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Geovibrionaceae; Denitrovibrio.
OX NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67824.1, ECO:0000313|Proteomes:UP000002012};
RN [1] {ECO:0000313|EMBL:ADD67824.1, ECO:0000313|Proteomes:UP000002012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12809 / NBRC 114555 / N2460
RC {ECO:0000313|Proteomes:UP000002012};
RX PubMed=21304711; DOI=10.4056/sigs.892105;
RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT (N2460).";
RL Stand. Genomic Sci. 2:270-279(2010).
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; CP001968; ADD67824.1; -; Genomic_DNA.
DR RefSeq; WP_013010355.1; NC_013943.1.
DR AlphaFoldDB; D4H6V8; -.
DR STRING; 522772.Dacet_1048; -.
DR PaxDb; 522772-Dacet_1048; -.
DR KEGG; dap:Dacet_1048; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_2_0_0; -.
DR InParanoid; D4H6V8; -.
DR OrthoDB; 9800746at2; -.
DR Proteomes; UP000002012; 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 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:ADD67824.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002012}.
FT DOMAIN 3..54
FT /note="Nitrogenase molybdenum-iron protein beta chain N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF11844"
FT DOMAIN 68..485
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 503 AA; 56922 MW; 423DC0BA26A88150 CRC64;
MSEKLNIKDH IELFKREDYI ELFENKKKYE GGESDERIQE ILEWTKTEEY KKINFERKDL
VVNPLKACQP LGGYYAAIGF EKTMPFVHGS QGCASYFRSH FMRHFREPFP GSCDAMTEDA
AVFGGHNALY LGLQNTYELF KPEMIAICTS CMAEVIGDDL NNFVKNAKNE GYIPEDFPVT
YAHTPSFVGS HVVGYDAMIA AILTQLGELK EEKNDKINVV MGFDTYVANY DEIKRIFKLF
GAELNLISDP SEVLNSPADG EYKMYYGGTP LADVKDAPNA KSAILMQKYS LLKTKELLEG
WGQEVKVVSP YGIEGTDELM MALSELTGKP VPAELEKERG QLVDAIGDSY YWVHGKTFGI
NGDPDFSLAL SRFVMELGGE PVHVLVTNGS KTWGKECDAL LQSSEYGKGG KAYPQKDMWH
YRSLLFTEPV DYMIGNSYGK FLERDTGIPL IRMGFPLQDR HHLHRYPTLG YKGGVQMLTW
IVNEILDDID FRTKDSASYD LLR
//
