ID A0A1T4P2I4_9ACTN Unreviewed; 313 AA.
AC A0A1T4P2I4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NAD-dependent formate dehydrogenase iron-sulfur protein {ECO:0000313|EMBL:SJZ85723.1};
GN ORFNames=SAMN02745673_01600 {ECO:0000313|EMBL:SJZ85723.1};
OS Marinactinospora thermotolerans DSM 45154.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Marinactinospora.
OX NCBI_TaxID=1122192 {ECO:0000313|EMBL:SJZ85723.1, ECO:0000313|Proteomes:UP000190637};
RN [1] {ECO:0000313|EMBL:SJZ85723.1, ECO:0000313|Proteomes:UP000190637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45154 {ECO:0000313|EMBL:SJZ85723.1,
RC ECO:0000313|Proteomes:UP000190637};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; FUWS01000004; SJZ85723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4P2I4; -.
DR STRING; 1122192.SAMN02745673_01600; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000190637; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 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; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000190637}.
FT DOMAIN 12..90
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 212..241
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 255..311
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 126..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 34263 MW; 34128E55DAC0588A CRC64;
MNTPVPLAPP RRLVDVTVDG QEVRVPEGAT IMQACAQTGV SCPTLCYGDT LTPKNACRIC
VVEVEGARTL APACSRPVEP GMAVRTDSDR VRHARRTVLE LLGSSVDLST TPQAQEWMEH
YDARPERFGP RAAPAPMGER DARRAGEHEP PTGAVAETVE QPAKIDNDLY VRDYGKCILC
YKCVDACGEQ WQNTFAIGVA GRGFDARVST EHDVALPDSA CVYCGNCIEV CPTGALSFKS
EFDMRAEGTW DESRQRQTTT VCTYCGVGCN VTLHVQDNEI VKVTSPHDNP VTHGNLCIKG
RFGFQHVQQR RHD
//