ID A6TTX9_ALKMQ Unreviewed; 454 AA.
AC A6TTX9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=Amet_3520 {ECO:0000313|EMBL:ABR49647.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR49647.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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; CP000724; ABR49647.1; -; Genomic_DNA.
DR RefSeq; WP_012064610.1; NC_009633.1.
DR AlphaFoldDB; A6TTX9; -.
DR STRING; 293826.Amet_3520; -.
DR KEGG; amt:Amet_3520; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_2_0_9; -.
DR OrthoDB; 9800746at2; -.
DR Proteomes; UP000001572; 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 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:ABR49647.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001572}.
FT DOMAIN 23..437
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 454 AA; 49591 MW; 60BC8ECC8CFDA43A CRC64;
MLDHTSKEIS ERKALVINPA KTCQPIGAMY AALGIHNCLP HSHGSQGCCS FHRMHLTRHF
RDPIVASTSS FTEGASVFGG SANLKTSIKN VFSVYKPDVI AINTTCLSET IGDDLPSTIS
DSEIPEGKHV FHANTPSYAG SHVTGFSNMV KAMVTHFSEG TGDGSNNKVN LIPGYTEPGD
MREIKRIAKL LDIPNILFPD TSGVVDSPMT GKYNMYPKGG TKVVELIDTG SSMATVALGK
FASEAAANEL EKKCKVASHP LNLPIGVKAT DEFIMELVKI TGKDVPDELE EERGMLVDIM
TDTHHHYHGK RVAIFGDPDH VMALTEFTLS LGMKPVYVVT GTPGKAFEKE VNGMLESSNV
EGRVKASGDL FELHQWVKNE PVDLLIGNTY GKYIARAEDI PLVRFGFPNM DRSIHSYFPV
VGYKGAMRLM EMIGNALLER VDRDALDEDF ELVL
//
