ID B7IGN5_THEAB Unreviewed; 658 AA.
AC B7IGN5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Hydrogenase-1 {ECO:0000313|EMBL:ACJ75249.1};
GN OrderedLocusNames=THA_787 {ECO:0000313|EMBL:ACJ75249.1};
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=484019 {ECO:0000313|EMBL:ACJ75249.1, ECO:0000313|Proteomes:UP000002453};
RN [1] {ECO:0000313|EMBL:ACJ75249.1, ECO:0000313|Proteomes:UP000002453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B {ECO:0000313|EMBL:ACJ75249.1,
RC ECO:0000313|Proteomes:UP000002453};
RX PubMed=19124572; DOI=10.1128/JB.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(2009).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP001185; ACJ75249.1; -; Genomic_DNA.
DR RefSeq; WP_012579795.1; NC_011653.1.
DR AlphaFoldDB; B7IGN5; -.
DR STRING; 484019.THA_787; -.
DR KEGG; taf:THA_787; -.
DR eggNOG; COG1905; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR eggNOG; COG4624; Bacteria.
DR HOGENOM; CLU_018240_2_1_0; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000002453; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02980; TRX_Fd_family; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.1780; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 4.10.260.20; Iron hydrogenase, small subunit; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR003149; Fe_hydrogenase_ssu.
DR InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11615:SF6; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11615; NITRATE, FORMATE, IRON DEHYDROGENASE; 1.
DR Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF02256; Fe_hyd_SSU; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00902; Fe_hyd_SSU; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53920; Fe-only hydrogenase; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1..76
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 76..115
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 133..164
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 177..206
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 658 AA; 73474 MW; A1F747F81B3DC49F CRC64;
MKIIVNGKET IIKDDSRNLL EALRDIGIEI PNLCYLSETS IYGACRMCLV EIDGQIMTSC
SIKPYEGMNV RTHTPEIYEM RRGILELILA SHNRDCTTCE RNGNCKLQRY AEEFGIRKIR
FDKLDKSNII DYSSIIIRDN SKCILCGDCV RVCDEIQSIG AIDFAFRGFE AQVMPAFGDE
LSTTNCVLCG QCVAHCPTGA LTFRNDLQNV YKAMEEGKYI IGMMAPAVRA SIQEELGMED
DVVVAGRIVN FLKSIGFKKV FDVAFAADLV AYEEAHEFKE RLEKGEKLPQ FTSCCPGWVK
FAEHNYPEYL NNLSTVKSPQ QALGSIIKKF YAKEIGVNPE DIYLVSIMPC TAKKFEAERE
ELVGEVDAVI TTRELSQLIR SSGFNLKNVP PVPFDRPYGL SSQSGLSFGK TGGVFGSVLK
VLESEIEFDD IKTEEIEKGI RVTKATTKDG KVISGVVVFG LGNTRKVIDS IKNGKLKVDI
VEVMACDYGC IGGGGQPYPN DARVRTKRAK ILNEVVGIDV LISPNENYHM LSLYERYLEK
PLSHVSHEVL HTTYRNRKRI NDEDIEILPL PVEEDKKTTV KVCLGTSCYS KGSYDILSDL
IDVVNKEEWA KNVEIKGTFC VENCGKSPNV VIDDTIVSEA TTEKVKEVLK KHVKSEKG
//
