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Database: UniProt
Entry: A4TZV4_9PROT
LinkDB: A4TZV4_9PROT
Original site: A4TZV4_9PROT 
ID   A4TZV4_9PROT            Unreviewed;       508 AA.
AC   A4TZV4;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ORFNames=MGR_1432 {ECO:0000313|EMBL:CAM76161.1};
OS   Magnetospirillum gryphiswaldense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM76161.1};
RN   [1] {ECO:0000313|EMBL:CAM76161.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MSR-1 {ECO:0000313|EMBL:CAM76161.1};
RX   PubMed=17449609; DOI=10.1128/JB.00119-07;
RA   Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA   Reinhardt R., Schueler D.;
RT   "Comparative genome analysis of four magnetotactic bacteria reveals a
RT   complex set of group-specific genes implicated in magnetosome
RT   biomineralization and function.";
RL   J. Bacteriol. 189:4899-4910(2007).
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; CU459003; CAM76161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TZV4; -.
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}.
FT   DOMAIN          1..56
FT                   /note="Nitrogenase molybdenum-iron protein beta chain N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11844"
FT   DOMAIN          70..491
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
SQ   SEQUENCE   508 AA;  55903 MW;  23A6366179C60827 CRC64;
     MPQSADKVKD HISLFKEPEY LELFASKKAQ FECRPTDEAV AAQAEYTKTW EYREKNFARE
     IATINPAKAC QPLGAVFVAA GFEGTLPYVH GSQGCVAYFR SHLARHFKEA VPIVADSMTE
     DAAVFGGLAN IVEGLQNAYT LYKPKMIVVS TTCMAEVIGD DLSAFIATAK EKESVPADFP
     VPFAHTPSFV GSHTTGYDNQ MKGILSYFWD REAQLTAAAG AKINIIPGFD GYAVANNREI
     KRYLDTMGVD YTFIGDVSDV YDTPSDGEYR MYDGGTTLDD TRAAINAKAT IGLQEFCSLK
     TLEYVATKGQ QTAAFNYPMG IGATDAFLMK VSELTGKAIP ASIEKERGRL VDAITDSQAW
     LHGKKFAVFG DPDFTLAMSA FLMEMGAEPT HVLATNGGKE WEAKAKALLA SSPFGASGQV
     WAGKDLWHLR SLLFTEPTDF IIGSSYGKYL EKDTGIPLIR LTFPIFDRHH HHRFPTFGYQ
     GALRVLVEIL DRVFEVADES DISFDLTR
//
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