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Database: UniProt
Entry: A0A258TQL1_9PROT
LinkDB: A0A258TQL1_9PROT
Original site: A0A258TQL1_9PROT 
ID   A0A258TQL1_9PROT        Unreviewed;       969 AA.
AC   A0A258TQL1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:OYY93741.1};
GN   ORFNames=B7Y41_09715 {ECO:0000313|EMBL:OYY93741.1};
OS   Hydrogenophilales bacterium 28-61-23.
OC   Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX   NCBI_TaxID=1970530 {ECO:0000313|EMBL:OYY93741.1, ECO:0000313|Proteomes:UP000215898};
RN   [1] {ECO:0000313|EMBL:OYY93741.1, ECO:0000313|Proteomes:UP000215898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=28-61-23 {ECO:0000313|EMBL:OYY93741.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:OYY93741.1}.
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DR   EMBL; NCGJ01000008; OYY93741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A258TQL1; -.
DR   Proteomes; UP000215898; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02783; MopB_CT_2; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
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:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          17..73
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   969 AA;  108663 MW;  AD2773143E256946 CRC64;
     MTQTLTASKS EPAALHEEVR TTTCYMCACR CGIKVHLKNG EVRFIEGNID HPLNQGVLCA
     KGSSGIMKQY SPARLTRPLR RKAGADRGVG EFEPISWDEA FAILEERLGK IRATDPKKFA
     LFTGRDQMQA LTGLFARQFG TPNYAAHGGF CSVNMAAGLI YTIGGSFWEF GGPDLDRAKL
     FVMLGTAEDH HSNPMKIALS KFKRDGGRFI SINPVRTGYS AIADEWIPIK PGTDGALLLA
     LIHEIIKQGL YDREFLVQYS NSAELVNIDA KSHEEGMFVR FEVPPEEGCF DPQNKLWWDR
     EMDRPVGTHT PGVDPYLLGE FKLADGTPVK PAFQLLAERV EQYTPEWAAG ITGIPVETIR
     RLAHEMGVTA RDQKIELPIA WTDVWDNEHK TITGNPVAFH AMRGLAAHSN GFHGIRALGI
     LMSLLGTIDR PGGFRHKAPF PRPIPPCAKT PTTPEAVRPN TPLDGMPLGW PADPDDLFVD
     DDGGPVRIDK AFSWEYPLSV HGLMHNVITN AWRGDPYKID TLLIFMANMA WNSTMNAVEV
     RKMLNDKEED GSYKIPFIVV ADAFQSEMTA FADLILPDTT YLERHDAMSM LDRPISEFDG
     PVDSVRIPVL PPTGECKPFQ EVLIELGSRL KLPAFTTKEG NRKFRDYPDF IVNFETAPGS
     GIGFLAGWRG KGGEKSMKGE PNPNQWQMYE QNNCVFQYHL PKSYQYMRNW NQGYLQWAQA
     HGMTRHSEPI NIHIYSEVLQ KFRLAAQGKT DGRQPPAHLK KRIETYFDPL PFYYEPLEAT
     LSDKHKYPLN AVTQRPMAMY HSWDSQNAWL RQIHAYNYLH INPKTAAAQG IADDDWIWIE
     SMHGKVRCMA RLSEAVEPGT VWTWNAIGKA AGAWNLDKDA NESKQGFLLN HLISEELPRN
     EAGEHISNSD PVTGQAAWYD VRVRIYKAGA DEPKETWPQF TAVPAAPGTP GRRPWQNYVA
     GLFGKGEGK
//
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