ID A0A162MUZ6_9FIRM Unreviewed; 578 AA.
AC A0A162MUZ6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Iron hydrogenase 1 {ECO:0000313|EMBL:KYO67778.1};
DE EC=1.12.7.2 {ECO:0000313|EMBL:KYO67778.1};
GN ORFNames=ATZ99_04180 {ECO:0000313|EMBL:KYO67778.1};
OS Thermovenabulum gondwanense.
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermovenabulum.
OX NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO67778.1, ECO:0000313|Proteomes:UP000075737};
RN [1] {ECO:0000313|EMBL:KYO67778.1, ECO:0000313|Proteomes:UP000075737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R270 {ECO:0000313|EMBL:KYO67778.1,
RC ECO:0000313|Proteomes:UP000075737};
RA Patel B.K.;
RT "Draft genome of Thermovenabulum gondwanense isolated from a red
RT thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO67778.1}.
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DR EMBL; LOHZ01000020; KYO67778.1; -; Genomic_DNA.
DR RefSeq; WP_068747596.1; NZ_LOHZ01000020.1.
DR AlphaFoldDB; A0A162MUZ6; -.
DR STRING; 520767.ATZ99_04180; -.
DR PATRIC; fig|520767.4.peg.428; -.
DR OrthoDB; 9798098at2; -.
DR Proteomes; UP000075737; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 1.10.15.40; Electron transport complex subunit B, putative Fe-S cluster; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR007202; 4Fe-4S_dom.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR11615:SF368; HYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11615; NITRATE, FORMATE, IRON DEHYDROGENASE; 1.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF04060; FeS; 1.
DR Pfam; PF00989; PAS; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53920; Fe-only hydrogenase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS51656; 4FE4S; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS50112; PAS; 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};
KW Oxidoreductase {ECO:0000313|EMBL:KYO67778.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075737}.
FT DOMAIN 2..30
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 31..60
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 361..423
FT /note="4Fe-4S"
FT /evidence="ECO:0000259|PROSITE:PS51656"
FT DOMAIN 414..484
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
SQ SEQUENCE 578 AA; 65946 MW; 3898250DF0E14EFA CRC64;
MEVINFTRAE CRNCYKCVRN CPVKAIRIKE GQAEIVLERC ITCGTCLIKC PQNAKTVKSD
MDKVNDILGK NEKVAVSLAP SFAGIFSSFN PENFMSRLKE LGFKDIFPTS QGAILIAKAY
ANIYNDKSRK VIISSACPAA NYLVQKYYPE LINYLVPVVS PMIAHGMYLK RVRGYSKVIF
IGPCLAKKME AMEFKEIIDA VITFDELKKL MGLKELIEET YFSENDDEEE NEEISIKTGA
ALYPIPGETV KTFSPFIKER WRREITVHGL DDLGEVFEEI KKGKLKDVFI EANACRGGCS
SGPATGDKKK DRFMKLGKIR EYAGRLKDKF QFENKNEELD MKAITREFTV LTVSKKIPSE
EEIRNILRQI GKYSERDELN CGTCGYDSCR EKAIAVYNGM AEIYMCIPYM RTRAESISEL
IIESTPNAIV VVDKNLQIQE YNPAAEKMFK KTKKEIIGMP LDYIFNDDDF RFVAELKENI
IAKKVKLPEY NLVTLQSIYF LHGHDLIIGI ISDITKQEED RKRNLEIKKK TIETTQQVIE
KQMRVAQEIA SVLGETTAET KVLLNRIKSI LKEELPDE
//
