GenomeNet

Database: UniProt
Entry: Q9ZRI8
LinkDB: Q9ZRI8
Original site: Q9ZRI8 
ID   FDH_HORVU               Reviewed;         377 AA.
AC   Q9ZRI8;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   13-FEB-2019, entry version 97.
DE   RecName: Full=Formate dehydrogenase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|PubMed:9489019};
DE            Short=FDH {ECO:0000255|HAMAP-Rule:MF_03210};
DE            EC=1.17.1.9 {ECO:0000255|HAMAP-Rule:MF_03210};
DE   AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210};
DE   Flags: Precursor;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ehimehadaka No.1; TISSUE=Root;
RX   PubMed=9489019; DOI=10.1104/pp.116.2.725;
RA   Suzuki K., Itai R., Suzuki K., Nakanishi H., Nishizawa N.K.,
RA   Yoshimura E., Mori S.;
RT   "Formate dehydrogenase, an enzyme of anaerobic metabolism, is induced
RT   by iron deficiency in barley roots.";
RL   Plant Physiol. 116:725-732(1998).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to
CC       carbon dioxide. Involved in the cell stress response.
CC       {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: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03210}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03210}.
DR   EMBL; D88272; BAA36181.1; -; mRNA.
DR   ProteinModelPortal; Q9ZRI8; -.
DR   SMR; Q9ZRI8; -.
DR   IntAct; Q9ZRI8; 1.
DR   PRIDE; Q9ZRI8; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   eggNOG; COG1052; LUCA.
DR   GO; GO:0005739; C:mitochondrion; 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; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; NAD; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     29       Mitochondrion. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   CHAIN        30    377       Formate dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000007194.
FT   NP_BIND     255    259       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   NP_BIND     331    334       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   REGION       30    145       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      146    332       Coenzyme-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      333    376       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     121    121       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     145    145       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     146    146       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     220    220       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     281    281       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     307    307       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        283    283       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        331    331       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
SQ   SEQUENCE   377 AA;  41546 MW;  E28C1FE24E9225C7 CRC64;
     MAAMWRAAAR QLVDRAVGSR AAHTSAGSKK IVGVFYQAGE YADKNPNFVG CVEGALGIRD
     WLESKGHHYI VTDDKEGFNS ELEKHIEDMH VLITTPFHPA YVTAEKIKKA KTPELLLTAG
     IGSDHIDLPA AAAAGLTVAR VTGSNTVSVA EDELMRILIL LRNFLPGYQQ VVKGEWNVAG
     IAHRAYDLEG KTVGTVGAGR YGRLLLQRLK PFNCNLLYHD RLQINPELEK EIGAKFEEDL
     DAMLPKCDVV VINTPLTEKT RGMFNKEKIA KMKKGVIIVN NARGAIMDTQ AVADACSSGH
     IAGYGGDVWF PQPAPKDHPW RYMPNHAMTP HISGTTIDAQ LRYAAGVKDM LDRYFKGEEF
     PVENYIVKEG ELASQYK
//
DBGET integrated database retrieval system