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Database: UniProt
Entry: W8V6M9_KLEPN
LinkDB: W8V6M9_KLEPN
Original site: W8V6M9_KLEPN 
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
//
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