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Database: UniProt
Entry: A0A0C3S4L6_PHLGI
LinkDB: A0A0C3S4L6_PHLGI
Original site: A0A0C3S4L6_PHLGI 
ID   A0A0C3S4L6_PHLGI        Unreviewed;       358 AA.
AC   A0A0C3S4L6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   28-MAR-2018, entry version 19.
DE   RecName: Full=Formate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03210};
DE            Short=FDH {ECO:0000256|HAMAP-Rule:MF_03210};
DE            EC=1.17.1.9 {ECO:0000256|HAMAP-Rule:MF_03210};
DE   AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03210};
GN   ORFNames=PHLGIDRAFT_25241 {ECO:0000313|EMBL:KIP05092.1};
OS   Phlebiopsis gigantea 11061_1 CR5-6.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Phanerochaetaceae; Phlebiopsis.
OX   NCBI_TaxID=745531 {ECO:0000313|EMBL:KIP05092.1, ECO:0000313|Proteomes:UP000053257};
RN   [1] {ECO:0000313|EMBL:KIP05092.1, ECO:0000313|Proteomes:UP000053257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11061_1 CR5-6 {ECO:0000313|EMBL:KIP05092.1,
RC   ECO:0000313|Proteomes:UP000053257};
RX   PubMed=25474575;
RA   Hori C., Ishida T., Igarashi K., Samejima M., Suzuki H., Master E.,
RA   Ferreira P., Ruiz-Duenas F.J., Held B., Canessa P., Larrondo L.F.,
RA   Schmoll M., Druzhinina I.S., Kubicek C.P., Gaskell J.A., Kersten P.,
RA   St John F., Glasner J., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J., Mgbeahuruike A.C., Kovalchuk A., Asiegbu F.O., Lackner G.,
RA   Hoffmeister D., Rencoret J., Gutierrez A., Sun H., Lindquist E.,
RA   Barry K., Riley R., Grigoriev I.V., Henrissat B., Kues U., Berka R.M.,
RA   Martinez A.T., Covert S.F., Blanchette R.A., Cullen D.;
RT   "Analysis of the Phlebiopsis gigantea genome, transcriptome and
RT   secretome provides insight into its pioneer colonization strategies of
RT   wood.";
RL   PLoS Genet. 10:E1004759-E1004759(2014).
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:0000256|HAMAP-Rule:MF_03210}.
CC   -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_03210}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03210}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_03210}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03210}.
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DR   EMBL; KN840553; KIP05092.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0A0C3S4L6; -.
DR   EnsemblFungi; KIP05092; KIP05092; PHLGIDRAFT_25241.
DR   OMA; SQGHEYL; -.
DR   Proteomes; UP000053257; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
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:0042183; P:formate catabolic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000053257};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_03210};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03210,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053257}.
FT   DOMAIN       36    337       2-Hacid_dh. {ECO:0000259|Pfam:PF00389}.
FT   DOMAIN      127    298       2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}.
FT   NP_BIND     172    173       NAD. {ECO:0000256|HAMAP-Rule:MF_03210}.
FT   NP_BIND     228    232       NAD. {ECO:0000256|HAMAP-Rule:MF_03210}.
FT   NP_BIND     309    312       NAD. {ECO:0000256|HAMAP-Rule:MF_03210}.
FT   BINDING      93     93       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03210}.
FT   BINDING     117    117       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03210}.
FT   BINDING     193    193       NAD. {ECO:0000256|HAMAP-Rule:MF_03210}.
FT   BINDING     254    254       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03210}.
FT   BINDING     280    280       NAD. {ECO:0000256|HAMAP-Rule:MF_03210}.
FT   SITE        256    256       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03210}.
FT   SITE        309    309       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03210}.
SQ   SEQUENCE   358 AA;  39520 MW;  6CC353282263787C CRC64;
     MKVLAILYKG GDAAKQEPRL LGAVENELGI RSWLESQGHE YLVSDDKEGP NSFLHKNIVD
     ADIVITTPFH PGYLTKELLD KAKNLKLCVT AGVGSDHVDL NAAVEKGLEV LEVTGSNVVS
     VAEHVVMSIL LLVRNFVPAH EMIERGDWQV SDIARNAFDL EGKVVGTIGA GRIGYRVLQR
     LQPFNCKEFL YYDYNGLKPD AEKAINARRV EDLKEFVSQC DVVTINAPLH EGTRGLINAD
     LLKHFKKDAW LVNTARGAIC NAEDVAAAVK SGQLNGYAGD VWNVQPAPKE HPWRYMKNPL
     QGGNGMVPHY SGTTLDAQQR YASGTKQILE NFFNNKPQEP ANIIIAKKGY VTKAYGQR
//
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