ID W8V6M9_KLEPN Unreviewed; 559 AA.
AC W8V6M9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Formate dehydrogenase H {ECO:0000313|EMBL:AHM81872.1};
DE EC=1.1.99.33 {ECO:0000313|EMBL:AHM81872.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:AHM81872.1};
GN ORFNames=KPNJ2_05100 {ECO:0000313|EMBL:AHM81872.1};
OS Klebsiella pneumoniae 30684/NJST258_2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1420013 {ECO:0000313|EMBL:AHM81872.1, ECO:0000313|Proteomes:UP000019586};
RN [1] {ECO:0000313|EMBL:AHM81872.1, ECO:0000313|Proteomes:UP000019586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30684/NJST258_2 {ECO:0000313|EMBL:AHM81872.1};
RX PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J., Bonomo R.A.,
RA Musser J.M., Kreiswirth B.N.;
RT "Molecular dissection of the evolution of carbapenem-resistant multilocus
RT sequence type 258 Klebsiella pneumoniae.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
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DR EMBL; CP006918; AHM81872.1; -; Genomic_DNA.
DR AlphaFoldDB; W8V6M9; -.
DR KEGG; kps:KPNJ2_05100; -.
DR PATRIC; fig|1420013.3.peg.4785; -.
DR HOGENOM; CLU_000422_4_0_6; -.
DR Proteomes; UP000019586; Chromosome.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd02790; MopB_CT_Formate-Dh_H; 1.
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 Gene3D; 1.20.5.460; Single helix bin; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:AHM81872.1}.
FT DOMAIN 1..331
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 420..526
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 559 AA; 62551 MW; BCB95D9550652558 CRC64;
MSNAITEIDN TDLVFIFGYN PADSHPIVAN HVINAKRNGA KIIVCDPRKI ETARIADMHI
ALKNGSNIAL LNAIGHVIIE EDLYDKSFVA SRSEGFEEYR KIVEGYTPES VEEITGVSAQ
EIRACARMYA SAKSAAILWG MGVTQFYQGV ETVRSLTSLA ILTGNLGKPN VGVNPVRGQN
NVQGACDMGA LPDTYPGYQY VKFPENREKF AKAWGVESLP AHTGYRISEL PHRAAHGEVR
AAYIMGEDPL QTDAELSAVR KAFDDLELVI VQDIFMTKTA SAADVILPST SWGEHEGVYT
AADRGFQRFF KAVEPKWDLK TDWQIISEIA TRMGYPMHYN NTQEIWDELR HLCPDFYGAT
YEKMGELGYV MWPCRDESDA DQGTSYLFKE KFDTPNGLAQ FFTCDWVAPI DKLTDEYPMV
LSTVREVGHY SCRSMTGNCA ALAALADEPG YAQINTADAE RLGIEDEELV WVNSRKGRII
TRAQVSDRPN KGAVYMTYQW WIGACNELVS ENLSPITKTP EYKYCAVNVE RIADQRAAEQ
YVIDEYNKLK SRLRESAMG
//