ID   GDH2_SCHPO              Reviewed;        1106 AA.
AC   Q9USN5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable NAD-specific glutamate dehydrogenase;
DE            Short=NAD-GDH;
DE            EC=1.4.1.2;
GN   Name=gdh2; ORFNames=SPCC132.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: NAD(+)-dependent glutamate dehydrogenase which degrades
CC       glutamate to ammonia and alpha-ketoglutarate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC         NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAB58131.1; -; Genomic_DNA.
DR   PIR; T40931; T40931.
DR   RefSeq; NP_588149.1; NM_001023138.2.
DR   AlphaFoldDB; Q9USN5; -.
DR   SMR; Q9USN5; -.
DR   BioGRID; 275720; 15.
DR   STRING; 4896.SPCC132.04c.1; -.
DR   iPTMnet; Q9USN5; -.
DR   MaxQB; Q9USN5; -.
DR   PaxDb; Q9USN5; -.
DR   PRIDE; Q9USN5; -.
DR   EnsemblFungi; SPCC132.04c.1; SPCC132.04c.1:pep; SPCC132.04c.
DR   GeneID; 2539148; -.
DR   KEGG; spo:SPCC132.04c; -.
DR   PomBase; SPCC132.04c; gdh2.
DR   VEuPathDB; FungiDB:SPCC132.04c; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   HOGENOM; CLU_005220_0_0_1; -.
DR   InParanoid; Q9USN5; -.
DR   OMA; LYCLPQN; -.
DR   PhylomeDB; Q9USN5; -.
DR   PRO; PR:Q9USN5; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:PomBase.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; EXP:PomBase.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028971; NAD-GDH.
DR   InterPro; IPR016210; NAD-GDH_euk.
DR   Pfam; PF05088; Bac_GDH; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   PIRSF; PIRSF000184; GDH_NAD; 1.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..1106
FT                   /note="Probable NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000310353"
FT   ACT_SITE        654
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1106 AA;  125712 MW;  5AFFEAB84F1295CA CRC64;
     MYLTKQIPHY SRIHTTQLLT VVNHRTIPFK IRGSFSNCRR YSNFATVPLL ERPFKNKSKH
     NTARASRPFS TQKMLLTKSH PPNMYKDSVF FGYRPIVFSG KQDQKSKVIQ CLRTERKTIP
     DDLVEDEVDR FYNKLGLDDY YFQMEPVSII ADHIEIIYAA KIAAHASHAK EELNIHVKNE
     NEDLAIYLDS SPVTQPELDQ SSAVEESIST RYLDPFKLTD PTAYRVESFT SVTNIDRTST
     ENSNIYTYFV TKCDFVDNPK KDASPDVPTD IASVSDKTFL EKASDNTIEM YQDVMNSVLT
     RFGPVVRLFD YQGRSEIRLV VGYRRGSIFQ YFPSLSKLFR YYGLHSTRTY VEQFSNGVTI
     ISYNFKPELF KNAAVTSINE LFSQITREAS LLYCLPSTDF QPLFVSEKLS IQEVTYAHCV
     RIFCEHVMNK LGPEYSSLSA ILDHSNNIHA EILETIKRRL STLAFTRTKI HDTIMQYPGL
     VHTLFEQFYL EHAINHNSTP HLHRAKSATS LADEASTYSI TPMSATALMD LIQKTCTNEE
     DVSVMEMFVK FNTHLLKTNF FQTTKVALSF RFDPSFLDST QYKDPLYAMI MSIGNEFRGF
     HLRFRDVARG GIRLIKSANP EAFGLNARGL FDENYNLAKT QMLKNKDIPE GGAKGVILLG
     KDCQDKPELA FMKYIDSIID LLIVNKSQPL VDKLGKPEIL FMGPDENTAD LVNWATIHAH
     RRNAPWWKSF FTGKKPTMGG IPHDKYGMTS LSVRCYVEGI YKKLNITDPS KLTKVQTGGP
     DGDLGSNEIK LSNEKYIAVI DGSGVLYDPA GLDRTELLRL ADERKTIDHF DAGKLSPEGY
     RVLVKDTNLK LPNGEIVRNG TIFRNTAHLR YKADTFVPCG GRPNAININN VEQLIDDHGR
     PAFKYLVEGA NLFITQDAKS VLEKAGVIVI RDASANKGGV TSSSLEVLAS LSFDDASFKE
     NMCVHDGKVP TFYADYVNEV KRIIQRNANL EFEAIWKGHS ENKIPYTSLS NHLSTEIVKL
     DHDIYNYEKL WADVGFRNAV LRASIPKTLQ AKIGLEKMLE RIPESYLRAI FSTYLASRFV
     YQHVVSSDPF AFFDYISTEM KMLKDA