ID   FDH_NEUCR               Reviewed;         375 AA.
AC   Q07103; Q7RVC9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-JUN-2009, entry version 77.
DE   RecName: Full=Formate dehydrogenase;
DE            EC=1.2.1.2;
DE   AltName: Full=NAD-dependent formate dehydrogenase;
DE            Short=FDH;
GN   Name=fdh; ORFNames=99H12.160, NCU03813;
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=93285982; PubMed=8509325;
RA   Chow C.M., RajBhandary U.L.;
RT   "Developmental regulation of the gene for formate dehydrogenase in
RT   Neurospora crassa.";
RL   J. Bacteriol. 175:3703-3709(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22542210; PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Developmentally regulated. Expressed only
CC       during conidiation and early germination.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily.
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DR   EMBL; L13964; AAA99900.1; -; Genomic_DNA.
DR   EMBL; AL451018; CAC18252.1; -; Genomic_DNA.
DR   EMBL; AABX02000011; EAA31966.1; -; Genomic_DNA.
DR   PIR; A47117; A47117.
DR   RefSeq; XP_961202.1; -.
DR   HSSP; P33160; 2NAC.
DR   GeneID; 3877330; -.
DR   KEGG; ncr:NCU03813; -.
DR   NMPDR; fig|5141.1.peg.1047; -.
DR   BioCyc; NCRA-XX3-01:NCRA-XX3-01-007561-MON; -.
DR   BRENDA; 1.2.1.2; 266.
DR   GO; GO:0008863; F:formate dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-O...; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH.
DR   InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    375       Formate dehydrogenase.
FT                                /FTId=PRO_0000076026.
FT   COMPBIAS    364    374       Ala-rich.
FT   ACT_SITE    259    259       By similarity.
FT   ACT_SITE    312    312       Proton donor (By similarity).
SQ   SEQUENCE   375 AA;  40957 MW;  3073CB95FB204968 CRC64;
     MVKVLAVLYD GGKHGEEVPE LLGTIQNELG LRKWLEDQGH TLVTTCDKDG ENSTFDKELE
     DAEIIITTPF HPGYLTAERL ARAKKLKLAV TAGIGSDHVD LNAANKTNGG ITVAEVTGSN
     VVSVAEHVLM TILVLVRNFV PAHEQIQEGR WDVAEAAKNE FDLEGKVVGT VGVGRIGERV
     LRRLKPFDCK ELLYYDYQPL SAEKEAEIGC RRVADLEEML AQCDVVTINC PLHEKTQGLF
     NKELISKMKK GSWLVNTARG AIVVKEDVAE ALKSGHLRGY GGDVWFPQPA PQDHPLRYAK
     NPFGGGNAMV PHMSGTSLDA QKRYAAGTKA IIESYLSGKH DYRPEDLIVY GGDYATKSYG
     ERERAKAAAA AAKSA
//