GenomeNet

Database: RefSeq
Entry: XP_664129
LinkDB: XP_664129
Original site: XP_664129 
LOCUS       XP_664129                377 aa            linear   PLN 03-APR-2018
DEFINITION  FDH_EMENI Probable formate dehydrogenase (NAD-dependent formate
            dehydrogenase) (FDH) [Aspergillus nidulans FGSC A4].
ACCESSION   XP_664129
VERSION     XP_664129.1
DBLINK      BioProject: PRJNA13961
            BioSample: SAMN02953587
DBSOURCE    REFSEQ: accession XM_659037.1
KEYWORDS    RefSeq.
SOURCE      Aspergillus nidulans FGSC A4
  ORGANISM  Aspergillus nidulans FGSC A4
            Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
            Eurotiomycetes; Eurotiomycetidae; Eurotiales; Aspergillaceae;
            Aspergillus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Galagan,J.E., Calvo,S.E., Cuomo,C., Ma,L.J., Wortman,J.R.,
            Batzoglou,S., Lee,S.I., Basturkmen,M., Spevak,C.C., Clutterbuck,J.,
            Kapitonov,V., Jurka,J., Scazzocchio,C., Farman,M., Butler,J.,
            Purcell,S., Harris,S., Braus,G.H., Draht,O., Busch,S., D'Enfert,C.,
            Bouchier,C., Goldman,G.H., Bell-Pedersen,D., Griffiths-Jones,S.,
            Doonan,J.H., Yu,J., Vienken,K., Pain,A., Freitag,M., Selker,E.U.,
            Archer,D.B., Penalva,M.A., Oakley,B.R., Momany,M., Tanaka,T.,
            Kumagai,T., Asai,K., Machida,M., Nierman,W.C., Denning,D.W.,
            Caddick,M., Hynes,M., Paoletti,M., Fischer,R., Miller,B., Dyer,P.,
            Sachs,M.S., Osmani,S.A. and Birren,B.W.
  TITLE     Sequencing of Aspergillus nidulans and comparative analysis with A.
            fumigatus and A. oryzae
  JOURNAL   Nature 438 (7071), 1105-1115 (2005)
   PUBMED   16372000
REFERENCE   2  (residues 1 to 377)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (03-APR-2018) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Birren,B., Nusbaum,C., Abebe,A., Abouelleil,A., Adekoya,E.,
            Ait-zahra,M., Allen,N., Allen,T., An,P., Anderson,M., Anderson,S.,
            Arachchi,H., Armbruster,J., Bachantsang,P., Baldwin,J., Barry,A.,
            Bayul,T., Blitshsteyn,B., Bloom,T., Blye,J., Boguslavskiy,L.,
            Borowsky,M., Boukhgalter,B., Brunache,A., Butler,J., Calixte,N.,
            Calvo,S., Camarata,J., Campo,K., Chang,J., Cheshatsang,Y.,
            Citroen,M., Collymore,A., Considine,T., Cook,A., Cooke,P.,
            Corum,B., Cuomo,C., David,R., Dawoe,T., Degray,S., Dodge,S.,
            Dooley,K., Dorje,P., Dorjee,K., Dorris,L., Duffey,N., Dupes,A.,
            Elkins,T., Engels,R., Erickson,J., Farina,A., Faro,S., Ferreira,P.,
            Fischer,H., Fitzgerald,M., Foley,K., Gage,D., Galagan,J.,
            Gearin,G., Gnerre,S., Gnirke,A., Goyette,A., Graham,J.,
            Grandbois,E., Gyaltsen,K., Hafez,N., Hagopian,D., Hagos,B.,
            Hall,J., Hatcher,B., Heller,A., Higgins,H., Honan,T., Horn,A.,
            Houde,N., Hughes,L., Hulme,W., Husby,E., Iliev,I., Jaffe,D.,
            Jones,C., Kamal,M., Kamat,A., Kamvysselis,M., Karlsson,E.,
            Kells,C., Kieu,A., Kisner,P., Kodira,C., Kulbokas,E., Labutti,K.,
            Lama,D., Landers,T., Leger,J., Levine,S., Lewis,D., Lewis,T.,
            Lindblad-toh,K., Liu,X., Lokyitsang,T., Lokyitsang,Y., Lucien,O.,
            Lui,A., Ma,L.J., Mabbitt,R., Macdonald,J., Maclean,C., Major,J.,
            Manning,J., Marabella,R., Maru,K., Matthews,C., Mauceli,E.,
            Mccarthy,M., Mcdonough,S., Mcghee,T., Meldrim,J., Meneus,L.,
            Mesirov,J., Mihalev,A., Mihova,T., Mikkelsen,T., Mlenga,V.,
            Moru,K., Mozes,J., Mulrain,L., Munson,G., Naylor,J., Newes,C.,
            Nguyen,C., Nguyen,N., Nguyen,T., Nicol,R., Nielsen,C., Nizzari,M.,
            Norbu,C., Norbu,N., O'donnell,P., Okoawo,O., O'leary,S.,
            Omotosho,B., O'neill,K., Osman,S., Parker,S., Perrin,D.,
            Phunkhang,P., Piqani,B., Purcell,S., Rachupka,T., Ramasamy,U.,
            Rameau,R., Ray,V., Raymond,C., Retta,R., Richardson,S., Rise,C.,
            Rodriguez,J., Rogers,J., Rogov,P., Rutman,M., Schupbach,R.,
            Seaman,C., Settipalli,S., Sharpe,T., Sheridan,J., Sherpa,N.,
            Shi,J., Smirnov,S., Smith,C., Sougnez,C., Spencer,B., Stalker,J.,
            Stange-thomann,N., Stavropoulos,S., Stetson,K., Stone,C., Stone,S.,
            Stubbs,M., Talamas,J., Tchuinga,P., Tenzing,P., Tesfaye,S.,
            Theodore,J., Thoulutsang,Y., Topham,K., Towey,S., Tsamla,T.,
            Tsomo,N., Vallee,D., Vassiliev,H., Venkataraman,V., Vinson,J.,
            Vo,A., Wade,C., Wang,S., Wangchuk,T., Wangdi,T., Whittaker,C.,
            Wilkinson,J., Wu,Y., Wyman,D., Yadav,S., Yang,S., Yang,X.,
            Yeager,S., Yee,E., Young,G., Zainoun,J., Zembeck,L., Zimmer,A.,
            Zody,M. and Lander,E.
  TITLE     Direct Submission
  JOURNAL   Submitted (26-APR-2004) Whitehead Institute/MIT Center for Genome
            Research, 320 Charles Street, Cambridge, MA 02142, USA
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence is identical to EAA57865.
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Aspergillus nidulans FGSC A4"
                     /strain="FGSC A4"
                     /db_xref="taxon:227321"
                     /chromosome="I"
                     /map="unlocalized"
     Protein         1..377
                     /product="FDH_EMENI Probable formate dehydrogenase
                     (NAD-dependent formate dehydrogenase) (FDH)"
                     /calculated_mol_wt=41444
     Region          1..370
                     /region_name="FDH"
                     /note="NAD-dependent Formate Dehydrogenase (FDH); cd05302"
                     /db_xref="CDD:240627"
     Site            order(4..6,16,117..118,121..122,124..125,128..129,132,
                     134..135,137..142,144..153,155..159,161,177..178,181..182,
                     297,300..302,304,309..310,319..326,328..331,333,335)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240627"
     Region          26..351
                     /region_name="LdhA"
                     /note="Lactate dehydrogenase or related 2-hydroxyacid
                     dehydrogenase [Energy production and conversion, Coenzyme
                     transport and metabolism, General function prediction
                     only]; COG1052"
                     /db_xref="CDD:223980"
     Site            order(64..65,88..89,115)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240627"
     Site            order(65,89,115..116,119,167,169..171,191..193,224..226,
                     228,231,269..271,295..296,324,326..327)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240627"
     Site            order(271,300,324)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:240627"
     CDS             1..377
                     /locus_tag="AN6525.2"
                     /coded_by="XM_659037.1:1..1134"
                     /db_xref="GeneID:2870218"
ORIGIN      
        1 mvlydggsha kdqpgllgtt enelgirkwi eeqghtlvtt sdkdgenstf dkelvdaevi
       61 ittpfhpgyl taerlakakn lklavtagig sdhvdldaan ktnggitvae vtgsnvvsva
      121 ehvvmtilll vrnfvpahdq irngdwnvaa vaknefdlen kvvgtvgvgr igervlrrlk
      181 pfdckellyy dyqplrpeve keigarrvds leemvsqcdv vtincplhek trglfnkeli
      241 skmkpgksal lyliipmlmy hkgswlvnta rgaivvkedv aealksghlr gyggdvwfpq
      301 papkehplry aehpwgggna tvphmsgtsi daqiryangt kaildsyfsg rfdyqpqdli
      361 vhggdyatka ygqrekk
//
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