ID A0A388SES2_9BURK Unreviewed; 1040 AA.
AC A0A388SES2; A0A401LI92;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Formate dehydrogenase-N subunit alpha {ECO:0000313|EMBL:GBO94776.1};
GN Name=fdnG {ECO:0000313|EMBL:GBO94776.1};
GN ORFNames=MESMUL_21300 {ECO:0000313|EMBL:GBO94776.1};
OS Mesosutterella multiformis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Mesosutterella.
OX NCBI_TaxID=2259133 {ECO:0000313|EMBL:GBO94776.1, ECO:0000313|Proteomes:UP000266091};
RN [1] {ECO:0000313|EMBL:GBO94776.1, ECO:0000313|Proteomes:UP000266091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4NBBH2 {ECO:0000313|EMBL:GBO94776.1,
RC ECO:0000313|Proteomes:UP000266091};
RX PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT human faeces.";
RL Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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:GBO94776.1}.
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DR EMBL; BGZJ01000002; GBO94776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A388SES2; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000266091; 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; cd02792; MopB_CT_Formate-Dh-Na-like; 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; 2.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 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.
DR PROSITE; PS51318; TAT; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000266091};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1040
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030071297"
FT DOMAIN 44..100
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1040 AA; 117629 MW; 2F821C3FDA78397E CRC64;
MGISRRSFFK RSMALGTSGF VAAAPSLAHA AADTAKKPYK LVSTQEFTNI CCYCAGGCGV
ICSVRNGELV NLEGDPDHPV NKGGLCPKGA TMFNLRNVVT PDRKVKHNES RLLKPQVRRP
GSDKWEDISW EDAFNEIARH VKKTRDENFV EYEDGVLVNR NDGMASIGAA QLQTEEAWLV
QKFCRSLGSV QIDNQTRPCH SSTPAGFAPT FGRGSMTSHW CDIENADVVM SIGSNSVESH
PLSSRYIERA QRKGGTWIVV DPRYTRSAAQ ADLYACIRPG TDIAFFGGMM NYILSNNLWQ
DEYVKNYTNA PCLINPDFKF DPESGHFTGY NPDTHKYDDE TWSYQTASDR EWDTKGAMNW
VTKPGVPKFK YPTVHEPKKD MTLQDPNCVF QIMKRHYSRY TLDKVSSVTG IDKEVLEKVY
QVYTSTGKRE RVGTILYALG ETQHTFGSQN CRSMAVIQLL LGNVGVPGGG VNALRGEPNV
QGSTDIAATS DGLPGYLNYP RQDKHAKLAD WLAKETYADG YYTNKPKFMV SILKEWYGEN
ATVENDYGYD WMPKLPHEYR DASMIPTWNR MRDGKVKGYF VWGMNPAHFA PNASNARRGL
AKLDWMVVSD IVPTETSDFW KEPGFDVKSC KTEIYRLPAA LIYERPGSIV NSGRMLQWRE
QAVPPLGQAK WDLEMMSEIF TRVQDLYRKE GGKCPEAVTK VNWDYKVDGK WSMERVARAL
NGYNTVTGKF LKTYGDLQAD GTSACGCWIY VGYWNNDDAP LDHTKQPVYR RGTEDPSGLG
VFPNWAWVWP ANRRILYNRG AADMKGQPWN PKRDLLHWDE KAQKWVCYDV PDFVAAKDGK
GVPPNNKAFM MTWEQYSRLF PNHGMADGPL PEHYEPWESP VKNQINGSQN NPCAIYTNDP
SVKRADPDKF PIVATTYSVV EHWQAGGQTR NCPWLVEISP RPFVEMSEEL AKEKGIKNKD
LVRVWNNRGE VRVQAMVTKR LKPVMVDGKP HHILGCPHHF SFIGRYASDR WTMNDLTPNV
GDPNSQIPEY RGFLVNVEKA
//
