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Database: UniProt
Entry: Q03134
LinkDB: Q03134
Original site: Q03134 
ID   FDH_EMENI               Reviewed;         365 AA.
AC   Q03134; C8V0K7; Q5AYV5;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   16-JAN-2019, entry version 122.
DE   RecName: Full=Formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210};
DE            Short=FDH {ECO:0000255|HAMAP-Rule:MF_03210};
DE            EC=1.17.1.9 {ECO:0000255|HAMAP-Rule:MF_03210};
DE   AltName: Full=Acetate inducible protein A {ECO:0000303|PubMed:1465107};
DE   AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210};
GN   Name=aciA {ECO:0000303|PubMed:1465107}; ORFNames=AN6525;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=1465107; DOI=10.1007/BF00279380;
RA   Saleeba J.A., Cobbett C.S., Hynes M.J.;
RT   "Characterization of the amdA-regulated aciA gene of Aspergillus
RT   nidulans.";
RL   Mol. Gen. Genet. 235:349-358(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to
CC       carbon dioxide. Formate oxidation is the final step in the
CC       methanol oxidation pathway in methylotrophic microorganisms. Has a
CC       role in the detoxification of exogenous formate in non-
CC       methylotrophic organisms. {ECO:0000255|HAMAP-Rule:MF_03210}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.9; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03210};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03210}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03210}.
CC   -!- INDUCTION: Acetate induction mediated by the amdA regulatory gene.
CC       {ECO:0000269|PubMed:1465107}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03210}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA77687.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA57865.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; Z11612; CAA77687.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AACD01000109; EAA57865.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001301; CBF70916.1; -; Genomic_DNA.
DR   PIR; S30088; S30088.
DR   RefSeq; XP_664129.1; XM_659037.1.
DR   ProteinModelPortal; Q03134; -.
DR   SMR; Q03134; -.
DR   STRING; 162425.CADANIAP00007297; -.
DR   PRIDE; Q03134; -.
DR   EnsemblFungi; CBF70916; CBF70916; ANIA_06525.
DR   EnsemblFungi; EAA57865; EAA57865; AN6525.2.
DR   GeneID; 2870218; -.
DR   KEGG; ani:AN6525.2; -.
DR   HOGENOM; HOG000136703; -.
DR   InParanoid; Q03134; -.
DR   KO; K00122; -.
DR   OMA; EVTYCNS; -.
DR   OrthoDB; 700058at2759; -.
DR   Proteomes; UP000000560; Chromosome I.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006083; P:acetate metabolic process; IEP:AspGD.
DR   GO; GO:0042183; P:formate catabolic process; IBA:GO_Central.
DR   CDD; cd05302; FDH; 1.
DR   HAMAP; MF_03210; Formate_dehydrogenase; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR033689; FDH_NAD-dep.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 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; Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    365       Formate dehydrogenase.
FT                                /FTId=PRO_0000076024.
FT   NP_BIND     175    176       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   NP_BIND     231    235       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   NP_BIND     312    315       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   REGION        3    120       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      121    313       Coenzyme-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      314    359       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING      94     94       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     120    120       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     196    196       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     257    257       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     283    283       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        259    259       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        312    312       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
SQ   SEQUENCE   365 AA;  40131 MW;  C9AB2B4EFBFC540D CRC64;
     MGKVLMVLYD GGSHAKDQPG LLGTTENELG IRKWIEEQGH TLVTTSDKDG ENSTFDKELV
     DAEVIITTPF HPGYLTAERL AKAKNLKLAV TAGIGSDHVD LDAANKTNGG ITVAEVTGSN
     VVSVAEHVVM TILLLVRNFV PAHDQIRNGD WNVAAVAKNE FDLENKVVGT VGVGRIGERV
     LRRLKPFDCK ELLYYDYQPL RPEVEKEIGA RRVDSLEEMV SQCDVVTINC PLHEKTRGLF
     NKELISKMKP GSWLVNTARG AIVVKEDVAE ALKSGHLRGY GGDVWFPQPA PKEHPLRYAE
     HPWGGGNATV PHMSGTSIDA QIRYANGTKA ILDSYFSGRF DYQPQDLIVH GGDYATKAYG
     QREKK
//
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