ID M4MDV2_9CYAN Unreviewed; 114 AA.
AC M4MDV2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=nitrogenase {ECO:0000256|ARBA:ARBA00012773};
DE EC=1.18.6.1 {ECO:0000256|ARBA:ARBA00012773};
DE Flags: Fragment;
GN Name=nifH {ECO:0000313|EMBL:AGG68333.1};
OS Leptolyngbya saxicola LEGE 07132.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=945748 {ECO:0000313|EMBL:AGG68333.1};
RN [1] {ECO:0000313|EMBL:AGG68333.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LEGE 07132 {ECO:0000313|EMBL:AGG68333.1};
RX PubMed=22277323; DOI=10.1016/j.syapm.2011.07.003;
RA Brito A., Ramos V., Seabra R., Santos A., Santos C.L., Lopo M.,
RA Ferreira S., Martins A., Mota R., Frazao B., Martins R., Vasconcelos V.,
RA Tamagnini P.;
RT "Culture-dependent characterization of cyanobacterial diversity in the
RT intertidal zones of the Portuguese coast: a polyphasic study.";
RL Syst. Appl. Microbiol. 35:110-119(2012).
CC -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC catalyzed by the nitrogenase complex, which has 2 components: the iron
CC protein and the molybdenum-iron protein.
CC {ECO:0000256|ARBA:ARBA00002234}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC {ECO:0000256|ARBA:ARBA00005504, ECO:0000256|RuleBase:RU003688}.
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DR EMBL; KC256767; AGG68333.1; -; Genomic_DNA.
DR AlphaFoldDB; M4MDV2; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR030655; NifH/chlL_CS.
DR InterPro; IPR000392; NifH/frxC.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42864; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR PANTHER; PTHR42864:SF2; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR Pfam; PF00142; Fer4_NifH; 1.
DR PRINTS; PR00091; NITROGNASEII.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00746; NIFH_FRXC_1; 1.
DR PROSITE; PS00692; NIFH_FRXC_2; 1.
DR PROSITE; PS51026; NIFH_FRXC_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU003688};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003688};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003688};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU003688};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003688};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003688};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003688}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGG68333.1"
FT NON_TER 114
FT /evidence="ECO:0000313|EMBL:AGG68333.1"
SQ SEQUENCE 114 AA; 12213 MW; 61AD92B08FC68A85 CRC64;
DSTRLMLHSK AQTTILHLAA ERGAVEDLEL EEVLLTGYKD VKCVESGGPE PGVGCAGRGI
ITAINFLEEE GAYEDLDFVS YDVLGDVVCG GFAMPIREGK AQEIYIVTSG EMMA
//
