ID C1D4K2_LARHH Unreviewed; 806 AA.
AC C1D4K2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Formate dehydrogenase-O, major subunit {ECO:0000313|EMBL:ACO73796.1};
DE EC=1.17.1.9 {ECO:0000313|EMBL:ACO73796.1};
GN OrderedLocusNames=LHK_00803 {ECO:0000313|EMBL:ACO73796.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO73796.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO73796.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO73796.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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}.
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DR EMBL; CP001154; ACO73796.1; -; Genomic_DNA.
DR AlphaFoldDB; C1D4K2; -.
DR STRING; 557598.LHK_00803; -.
DR KEGG; lhk:LHK_00803; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_2_4; -.
DR Proteomes; UP000002010; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 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; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 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 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACO73796.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002010}.
FT DOMAIN 2..378
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 684..799
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 806 AA; 90310 MW; 90C2D523CEC6343E CRC64;
MTNHWVDIKN ADLVVIMGGN AAEAHPVGFR WVVEAKQTRG ARLVVVDPRF TRSASVADYY
APIRSGTDIA FLGGVINWLI SNDKINWEYV RQYTNAALLV RDDFAFNDGL FSGWDADKAK
YADKSSWDYQ RDENGYALRD DTLANPRCVW NLLKAHYARY TPEVVSNVTG TPQEQFLQVC
EMLGECARPD KVATFLYALG WTQHSIGSQN IRTMAMIQLL LGNMGMPGGG VNALRGHSNI
QGLTDLGLLS TNLPGYLNLP NEKVAGYEDY LAKSTPKEWL PGQMNYWQNT PKFFVSLMKA
FYGNAATAEN NWAFDWLPKW DKSYDVLQVF ELMHQGKING YMCQGFNPVA SFPNKNKVIE
SLSKLKFLVI MDPLVTDTST FWKNHGEQND VKTEDIQTEV FRLPTTCFAE EEGAIVNSGR
WLQWHWKGAD APGEARTDVE IMSGIYQQLK AAYAKEGGAL PDPVLNLSWQ YRDPHEPSAE
ELAKELNGKA LADLPDPKDP TRFLARKGEQ LSTFAHLQGD GTTASGCWIF TGSWTQAGNQ
MARRDNTDTG LGNTPGWSWA WPANRRIIYN RASMDRDGKP WDPARCQLKW NGEKWTGGDV
ADFKADEAPG SAMNPFIMQP EGMGRLFALD KMAEGPFPEH YEPFESPIGT NPLHPQVVSN
PAARVFKDDR AQFGTSEKFP YVGTTYRLTE HFHYWTKNSR LNAITQPEQF VEIGEVLARE
KGIAHGDMVK VSSNRGYIKA KAVVTKRIKP LTVDGKPVHH IGIPIHWGYE GVAKKGFIAN
TLTPFVGDAN TQTPEFKTFL VNVEKA
//
