ID Q2NFA1_METST Unreviewed; 262 AA.
AC Q2NFA1;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=NifH {ECO:0000313|EMBL:ABC57502.1};
DE EC=1.18.6.1 {ECO:0000313|EMBL:ABC57502.1};
GN Name=nifH {ECO:0000313|EMBL:ABC57502.1};
GN OrderedLocusNames=Msp_1120 {ECO:0000313|EMBL:ABC57502.1};
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860 {ECO:0000313|EMBL:ABC57502.1, ECO:0000313|Proteomes:UP000001931};
RN [1] {ECO:0000313|EMBL:ABC57502.1, ECO:0000313|Proteomes:UP000001931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3
RC {ECO:0000313|Proteomes:UP000001931};
RX PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC {ECO:0000256|ARBA:ARBA00005504, ECO:0000256|RuleBase:RU003688}.
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DR EMBL; CP000102; ABC57502.1; -; Genomic_DNA.
DR RefSeq; WP_011406701.1; NC_007681.1.
DR AlphaFoldDB; Q2NFA1; -.
DR STRING; 339860.Msp_1120; -.
DR GeneID; 41325690; -.
DR KEGG; mst:Msp_1120; -.
DR eggNOG; arCOG00590; Archaea.
DR HOGENOM; CLU_059373_0_0_2; -.
DR OrthoDB; 145464at2157; -.
DR Proteomes; UP000001931; Chromosome.
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 CDD; cd02040; NifH; 1.
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 NCBIfam; NF033200; F430_CfbC; 1.
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 PIRSF; PIRSF000363; Nitrogenase_iron; 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|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,
KW ECO:0000313|EMBL:ABC57502.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001931}.
SQ SEQUENCE 262 AA; 28523 MW; B7F71C4A74A277C9 CRC64;
MVLKKIAIYG KGGIGKSTTV SNMAAAYDNS TFVIGCDPKA DTTRTLVGKR IPTILDTMRD
NTQPELEDIV YEGYNNTLCV ESGGPEPGVG CAGRGVIVAM NLLDKIGAFD NDPDLVIYDV
LGDVVCGGFS VPLREDYADE VYIVTSGEYM SLYAANNIAK GIKKLNGKLG GIICNCRNVK
NEVEVVTEFA SLISSKIMGI IPRCELVQTS EYKASTVVET FPDSSQSKIY SELINNIMNN
QEFSTPTPMG IEEFEEFFYS YV
//
