ID A0A1C2G1T1_9GAMM Unreviewed; 949 AA.
AC A0A1C2G1T1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:OCX45345.1};
GN ORFNames=A9R16_12060 {ECO:0000313|EMBL:OCX45345.1}, C4900_10515
GN {ECO:0000313|EMBL:RCN56267.1};
OS Acidiferrobacter thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Acidiferrobacter.
OX NCBI_TaxID=163359 {ECO:0000313|EMBL:OCX45345.1};
RN [1] {ECO:0000313|EMBL:OCX45345.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZJ {ECO:0000313|EMBL:OCX45345.1};
RA Ma L.;
RT "Draft Genome Sequence of Acidiferrobacter thiooxydans ZJ, a Distinctive
RT Species of Ectothiorhodospiraceae.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RCN56267.1, ECO:0000313|Proteomes:UP000253250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=m-1 {ECO:0000313|Proteomes:UP000253250}, and M-1
RC {ECO:0000313|EMBL:RCN56267.1};
RA Issotta F., Thyssen C., Mena C., Moya A., Bellenberg S., Sproer C.,
RA Covarrubias P.C., Sand W., Quatrini R., Vera M.;
RT "Insights into the biology of acidophilic members of the
RT Acidiferrobacteraceae family derived from comparative genomic analyses.";
RL Submitted (FEB-2018) 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:OCX45345.1}.
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DR EMBL; MDCF01000119; OCX45345.1; -; Genomic_DNA.
DR EMBL; PSYR01000002; RCN56267.1; -; Genomic_DNA.
DR RefSeq; WP_065970434.1; NZ_PSYR01000002.1.
DR STRING; 163359.A9R16_12060; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000253250; 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; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 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 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.
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 13..69
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 426..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..441
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 106854 MW; A4FADE7FDDAEE6FA CRC64;
MSAPQHEHEH GTSEVKYSTC YMCACRCGIK VTIENNQVRF IQGNRNHPIN KGVLCAKGSA
GIMKQCSPAR LRSPLLRKPG TERGAGEFIE ISWDKALDIL TERLARIRAT DPNKFAFFTG
RDQMQALTRL FAEQFGTLNW SAHGGFCSVN MAAAGLYTLG YAFWEFGDPD WDRTKYFMLW
GVAEDHNSNP MKIGIEKLKS RGGKFVGINP ARTGYQAVAD EWVPIRPGTD AMLALSMIHV
LLSRDLFDWD FLIRYTNAPF LVVQTPGEKG DGLIYRDEAG QPLAWDLKKE AFVNGLDASC
HPALFGEYKT PDGRTVKTVM TLLAERYLDE RFAPVNAAKI CGVPAATIER LALEMAHVAF
KETIEVAVEW TDWAGRKHDK FIGRPVSMHA MRGVSAHSNG FQAARAIHFL QILLGTIDCP
GGFRAKPPYP RPVPSPGKPA RHSAPNTPLD AHPLGFPTAP EDLVIDDEGR PLRIDKAYSW
EAPIANHGLM HMVITNAVKG DPYPIDTLLF FMANMAWNSS MNTANIQDML RAKGPDGEYK
IPFLVVADAF HSETVHFADL VLPDTTYLER YDAISLLDRP ISEPDAVADS IRHPLLALDR
DVRPWQEVMI ELGARLKLPV FTNADGTPKY KGYKDFITYY EREPGIGFLA GYRGADGSKS
LRGEPNPQQW ERYIENQGFF QYHLPKGIRY MRFANKGYLE FAVEAGFLKT AEPIMIELYS
EAIQRFRLAG LGLYDGPTPK ERVDQERLAT YFDPLPDYYE PLEQQRVDKE EYPFFAVNQR
PMMMYHSWDS QNAWLRQIIA QNHLYMNRAR GESLGFKDGD WVWVESHNGK IRVQLRLIEA
CQEDTVWTWN AIGKQSGTWG LKPGGPEATE GFLMNHLISE LLPEKSGERR LTNSDPITGQ
AAWYDLRVKV TRAAPGEEGV WPTFANVPPL PGAPPKPDIL RYNTRTKAS
//
