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 03-AUG-2022, entry version 150.
DE RecName: Full=Glutamate synthase [NADH] {ECO:0000303|PubMed:7773104};
DE EC=1.4.1.14 {ECO:0000269|PubMed:7773104};
DE AltName: Full=Glutamine-oxoglutarate aminotransferase {ECO:0000303|PubMed:7773104};
DE Short=GOGAT {ECO:0000303|PubMed:7773104};
GN Name=glt1; ORFNames=SPAPB1E7.07;
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 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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=7773104; DOI=10.1007/bf00369864;
RA Perysinakis A., Kinghorn J.R., Drainas C.;
RT "Glutamine synthetase/glutamate synthase ammonium-assimilating pathway in
RT Schizosaccharomyces pombe.";
RL Curr. Microbiol. 30:367-372(1995).
RN [4]
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: Forms L-glutamate from L-glutamine and 2-oxoglutarate.
CC Represents an alternative pathway to L-glutamate dehydrogenase for the
CC biosynthesis of L-glutamate (PubMed:7773104). Participates with
CC glutamine synthetase in ammonia assimilation processes
CC (PubMed:7773104). The enzyme is specific for NADH, L-glutamine and 2-
CC oxoglutarate (PubMed:7773104). {ECO:0000269|PubMed:7773104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine +
CC NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58359; EC=1.4.1.14;
CC Evidence={ECO:0000269|PubMed:7773104};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000250|UniProtKB:Q12680};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:Q12680};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q12680};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q12680};
CC -!- ACTIVITY REGULATION: In the presence of 10 mM allantoin, the activity
CC is reduced more than 25%. {ECO:0000269|PubMed:7773104}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for glutamine {ECO:0000269|PubMed:7773104};
CC KM=0.07 mM for alpha-ketoglutarate {ECO:0000269|PubMed:7773104};
CC Vmax=0.05 umol/min/mg enzyme {ECO:0000269|PubMed:7773104};
CC pH dependence:
CC Optimum pH is 6.35. {ECO:0000269|PubMed:7773104};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:7773104};
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. {ECO:0000269|PubMed:7773104}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000269|PubMed:7773104}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q12680}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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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 AlphaFoldDB; Q9C102; -.
DR SMR; Q9C102; -.
DR BioGRID; 279927; 5.
DR STRING; 4896.SPAPB1E7.07.1; -.
DR iPTMnet; Q9C102; -.
DR MaxQB; Q9C102; -.
DR PaxDb; Q9C102; -.
DR PRIDE; Q9C102; -.
DR EnsemblFungi; SPAPB1E7.07.1; SPAPB1E7.07.1:pep; SPAPB1E7.07.
DR GeneID; 2543509; -.
DR KEGG; spo:SPAPB1E7.07; -.
DR PomBase; SPAPB1E7.07; glt1.
DR VEuPathDB; FungiDB:SPAPB1E7.07; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR InParanoid; Q9C102; -.
DR OMA; TVFRLQH; -.
DR PhylomeDB; Q9C102; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR PRO; PR:Q9C102; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA: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:0015930; F:glutamate synthase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019676; P:ammonia assimilation cycle; IMP:PomBase.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IDA:PomBase.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 2.160.20.60; -; 1.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
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; SSF56235; SSF56235; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR TIGRFAMs; TIGR01317; GOGAT_sm_gam; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3Fe-4S; Amino-acid biosynthesis; Cytoplasm; FAD; Flavoprotein; FMN;
KW Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..2111
FT /note="Glutamate synthase [NADH]"
FT /id="PRO_0000170789"
FT DOMAIN 69..469
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT REGION 969..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 1139..1191
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1192
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1198
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1203
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT CONFLICT 2067..2069
FT /note="CRR -> SA (in Ref. 2; BAA13827)"
FT /evidence="ECO:0000305"
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
