Entry sw:GLT1_SCHPO

ID   GLT1_SCHPO              Reviewed;        2111 AA.
AC   Q9C102; P78816;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   18-JAN-2017, entry version 121.
DE   RecName: Full=Putative glutamate synthase [NADPH];
DE            EC=1.4.1.13;
DE   AltName: Full=NADPH-GOGAT;
GN   Name=glt1; ORFNames=SPAPB1E7.07;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1923-2111.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [3]
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
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Forms L-glutamate from L-glutamine and 2-oxoglutarate.
CC       Represents an alternative pathway to L-glutamate dehydrogenase for
CC       the biosynthesis of L-glutamate. Participates with glutamine
CC       synthetase in ammonia assimilation processes. The enzyme is
CC       specific for NADH, L-glutamine and 2-oxoglutarate (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2 L-glutamate + NADP(+) = L-glutamine + 2-
CC       oxoglutarate + NADPH.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC       pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+)
CC       route): step 1/1.
CC   -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00609}.
DR   EMBL; CU329670; CAC36924.1; -; Genomic_DNA.
DR   EMBL; D89165; BAA13827.1; -; mRNA.
DR   PIR; T42527; T42527.
DR   RefSeq; NP_594133.1; NM_001019557.2.
DR   ProteinModelPortal; Q9C102; -.
DR   BioGrid; 279927; 2.
DR   MINT; MINT-4702166; -.
DR   MaxQB; Q9C102; -.
DR   PRIDE; Q9C102; -.
DR   EnsemblFungi; SPAPB1E7.07.1; SPAPB1E7.07.1:pep; SPAPB1E7.07.
DR   GeneID; 2543509; -.
DR   KEGG; spo:SPAPB1E7.07; -.
DR   EuPathDB; FungiDB:SPAPB1E7.07; -.
DR   PomBase; SPAPB1E7.07; glt1.
DR   HOGENOM; HOG000031559; -.
DR   InParanoid; Q9C102; -.
DR   KO; K00264; -.
DR   OMA; ETESSYI; -.
DR   OrthoDB; EOG092C00TJ; -.
DR   PhylomeDB; Q9C102; -.
DR   UniPathway; UPA00045; -.
DR   UniPathway; UPA00634; UER00690.
DR   PRO; PR:Q9C102; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016040; F:glutamate synthase (NADH) activity; IDA:PomBase.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0015930; F:glutamate synthase activity; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IDA:PomBase.
DR   GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02808; GltS_FMN; 1.
DR   Gene3D; 2.160.20.60; -; 1.
DR   Gene3D; 3.20.20.70; -; 2.
DR   Gene3D; 3.50.50.60; -; 3.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR002489; Glu_synth_asu_C.
DR   InterPro; IPR006982; Glu_synth_centr_N.
DR   InterPro; IPR012220; Glu_synth_euk.
DR   InterPro; IPR002932; Glu_synthdom.
DR   InterPro; IPR006005; Glut_synth_ssu1.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF00310; GATase_2; 1.
DR   Pfam; PF04898; Glu_syn_central; 1.
DR   Pfam; PF01645; Glu_synthase; 1.
DR   Pfam; PF01493; GXGXG; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF000187; GOGAT; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   SUPFAM; SSF69336; SSF69336; 1.
DR   TIGRFAMs; TIGR01317; GOGAT_sm_gam; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   2: Evidence at transcript level;
KW   3Fe-4S; Amino-acid biosynthesis; Complete proteome; Cytoplasm; FAD;
KW   Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase;
KW   Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1   2111       Putative glutamate synthase [NADPH].
FT                                /FTId=PRO_0000170789.
FT   DOMAIN       69    469       Glutamine amidotransferase type-2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00609}.
FT   NP_BIND    1139   1191       FMN. {ECO:0000250}.
FT   ACT_SITE     69     69       For GATase activity. {ECO:0000250}.
FT   METAL      1192   1192       Iron-sulfur (3Fe-4S). {ECO:0000250}.
FT   METAL      1198   1198       Iron-sulfur (3Fe-4S). {ECO:0000250}.
FT   METAL      1203   1203       Iron-sulfur (3Fe-4S). {ECO:0000250}.
FT   CONFLICT   2067   2069       CRR -> SA (in Ref. 2; BAA13827).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        69    492       ipfam:GATase_2 [T]
FT   MYHIT       530    815       ipfam:Glu_syn_central [T]
FT   MYHIT      1326   1512       ipfam:GXGXG [T]
FT   MYHIT      1634   1743       ipfam:Fer4_20 [T]
FT   MYHIT      1757   2078       ipfam:Pyr_redox_2 [T]
FT   MYHIT       876   1246       ipfam:Glu_synthase [T]
FT   MYHIT        69    469       iprf:GATASE_TYPE_2 [T]
SQ   SEQUENCE   2111 AA;  232849 MW;  D3CE58815CC4E158 CRC64;
     MAVLSSVQPI NHNSALVEAR DEQVNTTACS DDLLNAPPYE YDTEGNPSWA GALPKAQALY
     DPAYEKDSCG VGFTCHIKGQ VSHKIVTDAR LLLCNMTHRG ATGADTRDGD GAGVMTGMPY
     TFMQKEFGQI GCTLPKSGEY AIGNVFFSPE ADVCREAMTA FTQVAEKLGL AILAWRSVPC
     DNSILGPAAL SREPTILQPC VVLKAAYDGE AEFDTDLFER QLYVLRKQSS HLIGKEKWFY
     ICSLHRETIV YKGQLAPVQV YNYFLDLNNA EYVSHFALVH SRFSTNTFPS WDRAQPMRLA
     AHNGEINTLR GNKNWMHARE GLMKSSRFGE EFASLLPIIE RGGSDSAAFD NVIELLCASG
     VVSLPEAVML LIPEAWQNDK NISDEKAAFY EWAACQMEPW DGPALFTFAD GRYCGANLDR
     NGLRPCRFYL TSDDMMICAS EVGTVGIEPD RIVQKGRLYP GRMLLVDTKE GRIVDDKELK
     HNIASRYDFR SWLDQELIDM NSIVDSLIES TSVDLTPIVD DVPLADDKTM LAFGYTLEQI
     NMIMAPMANG GKETLGSMGN DAAIACLSDQ PRLLYDYFRQ LFAQVTNPPI DPIREAIVMS
     LQCYIGPSGN LLEINQSQCR RLRMPTPILT VEEFNALKNV DRIYPDWKVA SIDITFFKSE
     GVAGYAAAIE RICSEADTAV NEGYKAIVLS DRNVNSERVP LASIAACGAV HHYLVQNKLR
     SRVALVCESG DAREVHHMCT LLGYGADAVC PYLAMEALTK LVRQNAMKPG ITEETAIKNF
     KHAINGGILK VMSKMGISTL QSYKGAQIFE ALGIDNEVIN KCFLGTASRI RGVTFEHIAL
     DAFALHERGY PTDQSIRSLQ IPDMGDFYYR DGGEQHVNHP KAIASLQDAV RNKNEAAYAE
     FSRTHYEQTR RCTLRGMLDF DFDSSQAIPI EQVEPWTEIV RRFCTGAMSY GSISMESHSS
     LAIAMNRLGG KSNTGEGGED PARSQRLANG DTMRSAIKQI ASGRFGVTSW YLSDADELQI
     KMAQGAKPGE GGELPGNKVS ESIAKTRHST AGVGLISPPP HHDIYSIEDL KQLIYDMKSA
     NPRARVSVKL VSEVGVGIVA SGVAKAKADH ILVSGHDGGT GASRWTGIKY AGLPWELGVA
     ETHQTLVLND LRGRVVIQTD GQIRTGRDVA IACLLGAEEW GFATTPLIAL GCIMMRKCHL
     NTCPVGIATQ DPELRKKFEG QPEHVVNFFY YVAEELRGIM AKLGFRTINE MVGRSDKLKV
     AEPINNKSKL LDLTPLLTPA FTLRPGAATY NVRKQDHRLY TRLDNKLIDE AEVTLEEGIP
     SVVECEIINT DRTLGATLSN KISKRYGEEG LPTDSIRVNV FGSAGQSFGA FLAPGVTLQL
     EGDCNDYVGK GLSGGRLIIY PPRVSPFKPE ENMIIGNVCL YGATSGHAFI SGVAAERFAV
     RNSGAIAVVE GVGDHGCEYM TGGRVVILGS TGRNFAAGMS GGIAYVYDMQ MDFAGKINTE
     MVDISSVTDA AEIAFLRGLI QDHRHYTGSQ VADRILSDFP RHLSRFVKVL PREYKAVLER
     EAAKKEEAKR LQYPKAFMPG NPIRQQIEET NAQIADVEDT LGATVKKSAP LDKLRGFMKY
     QRRSEHYRNP LKRTNDWKEL SVRLREDELR VQTARCMDCG TPFCQSDYGC PISNKIFTWN
     DLVFKQQWKE ALTQLLLTNN FPEFTGRVCP APCEGACTLG IIESPVGIKS VERAIIDKAW
     EEGWIVPRPP AERTGRRVAI IGSGPAGLAA ADQLNRAGHH VVIYERADRP GGLLQYGIPN
     MKLDKKVVER RIQLMIDEGI EVLTNVEVGK NGDVSLDELH KVYDAVVLAS GSTVPRDLPI
     PNRDSKGIHF AMEFLHKNTK SLLDSELKDG NYISAKGKDV IVIGGGDTGN DCLGTSVRHG
     AKSVRNLELL PIPPRERAFD NPWPQYPRVF RVDYGHAEVQ AHYGQDFREY SILTKSFEKD
     EDGNVKGINT VRIEWTKNSK GRWIMKEIRN SEEFFPADLV ILALGFLGPE EQATAGMNVD
     RDARSNISTP TKSYETSVPG IYAAGDCRRG QSLVVWGIQE GRQCAREIDL KFQGKTFLPG
     DGGLVKRTVN C
//