ID D8GMG6_CLOLD Unreviewed; 453 AA.
AC D8GMG6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=nifK1 {ECO:0000313|EMBL:ADK13576.1};
GN OrderedLocusNames=CLJU_c04940 {ECO:0000313|EMBL:ADK13576.1};
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK13576.1, ECO:0000313|Proteomes:UP000001656};
RN [1] {ECO:0000313|EMBL:ADK13576.1, ECO:0000313|Proteomes:UP000001656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC
RC {ECO:0000313|Proteomes:UP000001656};
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform based
RT on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(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; CP001666; ADK13576.1; -; Genomic_DNA.
DR RefSeq; WP_013237176.1; NZ_LITS01000002.1.
DR AlphaFoldDB; D8GMG6; -.
DR STRING; 748727.CLJU_c04940; -.
DR KEGG; clj:CLJU_c04940; -.
DR PATRIC; fig|748727.19.peg.2165; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_2_0_9; -.
DR OrthoDB; 9800746at2; -.
DR Proteomes; UP000001656; 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 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:ADK13576.1}.
FT DOMAIN 23..436
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 453 AA; 50015 MW; 1C450AF932172E97 CRC64;
MLDATPKELV ERKQLRINPA KTCQPVGAMY AALGIHNCLP HSHGSQGCCS YHRTVLSRHF
KEPAMASTSS FTEGASVFGG GANVKKAVKN IFAMYNPDII AIHTTCLSET IGDDLPTYIR
EMEIPEGKLV IHANTPSYVG SHVTGFSNMV NGMVQYLSKS NGEKNGKFNI IPGFVGPADM
KEMKRIFKLM DIPYIIFPDT NGVFDTPNTG DYKMYPKGGT KIEDIVDAGN SDFTVAFGNY
ASELAAKSLE NKCKVPYKTL RAPIGIDAMD DLLMNLVRLT GKEVSAELEE ERGQLLDMMI
DSAQYFNGKK VAIVGDPDVV ISLTQFVITL GMIPKYVITG TPGSLFEKEI KAMMDEAGLE
GIAKANSDFF EMHQLIKNEG VDLLISNTYG KFIARAEDIP FVRFGFPVMD RYGHQYTPKV
GYYGAIKLVE SMLNAMLDKE ERECAEEDFE TVR
//
