ID W1SHB0_9BACI Unreviewed; 516 AA.
AC W1SHB0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:ETI67394.1};
GN ORFNames=BAVI_17837 {ECO:0000313|EMBL:ETI67394.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI67394.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI67394.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI67394.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(2014).
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:ETI67394.1}.
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DR EMBL; ALAN01000097; ETI67394.1; -; Genomic_DNA.
DR AlphaFoldDB; W1SHB0; -.
DR STRING; 220686.AA980_15955; -.
DR PATRIC; fig|1131730.3.peg.3748; -.
DR eggNOG; COG3383; Bacteria.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000018877; Unassembled WGS sequence.
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:InterPro.
DR Gene3D; 2.40.40.20; -; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018877}.
FT DOMAIN 1..314
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 403..510
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 516 AA; 58095 MW; FB4227BFA4F10DFC CRC64;
MGSNTTEAHP IIANRMKKAV KAGLKIIVID PRKIDMVKVA HRHLQINVGS DIALINAFIR
VILKEGLYNP EFIEQFTIDF DKLAKQVEPY TPEAAAAITG LKAEDIIATA REYANSSGSM
IAYTLGITEH HCGVNNVFDI ANLALLTGNI GKEGTGIMPL RGQNNVQGAG DMGCLPNQLA
GAMSLANEEF RARYEKVWKV ELNPQAGDTQ TRTFDRLEMG ELKALYIIGE NPLLADVNMN
HTKKLFEKLD LLIVQDIFMT ETAKMADVVL PARSWGEVDG TYTNTDRRIQ RVRKAIDAHP
NTKEDWEILC DLSTMMGYSM HYHNSEEIWD EVRKLAWEMY GGISYERLEK EYSIHYPCPD
ESHPGTFIMH QRFHTEQPME KKSPFVPVDY TEPLELPDAE YPFTLTTGRR YESYNTHTQT
RHYAAGVKVK QTEETVDIHP EDAAVLGITN GDIVQVRSRR GELEVKVKVT EQVVPGLVFM
SFHWSETPTN VLTLNEYDPI SGTAEYKACA VAISRV
//
