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Protein

Putative glutamate synthase [NADPH]

Gene

glt1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate (By similarity).By similarity

Catalytic activityi

2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: L-glutamate biosynthesis via GLT pathway

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+) route).
Proteins known to be involved in this subpathway in this organism are:
  1. Putative glutamate synthase [NADPH] (glt1)
This subpathway is part of the pathway L-glutamate biosynthesis via GLT pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+) route), the pathway L-glutamate biosynthesis via GLT pathway and in Amino-acid biosynthesis.

Pathwayi: nitrogen metabolism

This protein is involved in the pathway nitrogen metabolism, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway nitrogen metabolism and in Energy metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691For GATase activityBy similarity
Metal bindingi1192 – 11921Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1198 – 11981Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1203 – 12031Iron-sulfur (3Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1139 – 119153FMNBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Glutamate biosynthesis

Keywords - Ligandi

3Fe-4S, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00690.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative glutamate synthase [NADPH] (EC:1.4.1.13)
Alternative name(s):
NADPH-GOGAT
Gene namesi
Name:glt1
ORF Names:SPAPB1E7.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAPB1E7.07.
PomBaseiSPAPB1E7.07. glt1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21112111Putative glutamate synthase [NADPH]PRO_0000170789Add
BLAST

Proteomic databases

MaxQBiQ9C102.
PRIDEiQ9C102.

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

BioGridi279927. 1 interaction.
MINTiMINT-4702166.

Structurei

3D structure databases

ProteinModelPortaliQ9C102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 469401Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutamate synthase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000031559.
InParanoidiQ9C102.
KOiK00264.
OMAiHIAMLIG.
OrthoDBiEOG7TN012.
PhylomeDBiQ9C102.

Family and domain databases

Gene3Di2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.50.50.60. 3 hits.
3.60.20.10. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR028261. DPD_II.
IPR023753. FAD/NAD-binding_dom.
IPR017932. GATase_2_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR012220. Glu_synth_euk.
IPR002932. Glu_synthdom.
IPR006005. Glut_synth_ssu1.
IPR009051. Helical_ferredxn.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF14691. Fer4_20. 1 hit.
PF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000187. GOGAT. 1 hit.
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
TIGRFAMsiTIGR01317. GOGAT_sm_gam. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9C102-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVLSSVQPI NHNSALVEAR DEQVNTTACS DDLLNAPPYE YDTEGNPSWA
60 70 80 90 100
GALPKAQALY DPAYEKDSCG VGFTCHIKGQ VSHKIVTDAR LLLCNMTHRG
110 120 130 140 150
ATGADTRDGD GAGVMTGMPY TFMQKEFGQI GCTLPKSGEY AIGNVFFSPE
160 170 180 190 200
ADVCREAMTA FTQVAEKLGL AILAWRSVPC DNSILGPAAL SREPTILQPC
210 220 230 240 250
VVLKAAYDGE AEFDTDLFER QLYVLRKQSS HLIGKEKWFY ICSLHRETIV
260 270 280 290 300
YKGQLAPVQV YNYFLDLNNA EYVSHFALVH SRFSTNTFPS WDRAQPMRLA
310 320 330 340 350
AHNGEINTLR GNKNWMHARE GLMKSSRFGE EFASLLPIIE RGGSDSAAFD
360 370 380 390 400
NVIELLCASG VVSLPEAVML LIPEAWQNDK NISDEKAAFY EWAACQMEPW
410 420 430 440 450
DGPALFTFAD GRYCGANLDR NGLRPCRFYL TSDDMMICAS EVGTVGIEPD
460 470 480 490 500
RIVQKGRLYP GRMLLVDTKE GRIVDDKELK HNIASRYDFR SWLDQELIDM
510 520 530 540 550
NSIVDSLIES TSVDLTPIVD DVPLADDKTM LAFGYTLEQI NMIMAPMANG
560 570 580 590 600
GKETLGSMGN DAAIACLSDQ PRLLYDYFRQ LFAQVTNPPI DPIREAIVMS
610 620 630 640 650
LQCYIGPSGN LLEINQSQCR RLRMPTPILT VEEFNALKNV DRIYPDWKVA
660 670 680 690 700
SIDITFFKSE GVAGYAAAIE RICSEADTAV NEGYKAIVLS DRNVNSERVP
710 720 730 740 750
LASIAACGAV HHYLVQNKLR SRVALVCESG DAREVHHMCT LLGYGADAVC
760 770 780 790 800
PYLAMEALTK LVRQNAMKPG ITEETAIKNF KHAINGGILK VMSKMGISTL
810 820 830 840 850
QSYKGAQIFE ALGIDNEVIN KCFLGTASRI RGVTFEHIAL DAFALHERGY
860 870 880 890 900
PTDQSIRSLQ IPDMGDFYYR DGGEQHVNHP KAIASLQDAV RNKNEAAYAE
910 920 930 940 950
FSRTHYEQTR RCTLRGMLDF DFDSSQAIPI EQVEPWTEIV RRFCTGAMSY
960 970 980 990 1000
GSISMESHSS LAIAMNRLGG KSNTGEGGED PARSQRLANG DTMRSAIKQI
1010 1020 1030 1040 1050
ASGRFGVTSW YLSDADELQI KMAQGAKPGE GGELPGNKVS ESIAKTRHST
1060 1070 1080 1090 1100
AGVGLISPPP HHDIYSIEDL KQLIYDMKSA NPRARVSVKL VSEVGVGIVA
1110 1120 1130 1140 1150
SGVAKAKADH ILVSGHDGGT GASRWTGIKY AGLPWELGVA ETHQTLVLND
1160 1170 1180 1190 1200
LRGRVVIQTD GQIRTGRDVA IACLLGAEEW GFATTPLIAL GCIMMRKCHL
1210 1220 1230 1240 1250
NTCPVGIATQ DPELRKKFEG QPEHVVNFFY YVAEELRGIM AKLGFRTINE
1260 1270 1280 1290 1300
MVGRSDKLKV AEPINNKSKL LDLTPLLTPA FTLRPGAATY NVRKQDHRLY
1310 1320 1330 1340 1350
TRLDNKLIDE AEVTLEEGIP SVVECEIINT DRTLGATLSN KISKRYGEEG
1360 1370 1380 1390 1400
LPTDSIRVNV FGSAGQSFGA FLAPGVTLQL EGDCNDYVGK GLSGGRLIIY
1410 1420 1430 1440 1450
PPRVSPFKPE ENMIIGNVCL YGATSGHAFI SGVAAERFAV RNSGAIAVVE
1460 1470 1480 1490 1500
GVGDHGCEYM TGGRVVILGS TGRNFAAGMS GGIAYVYDMQ MDFAGKINTE
1510 1520 1530 1540 1550
MVDISSVTDA AEIAFLRGLI QDHRHYTGSQ VADRILSDFP RHLSRFVKVL
1560 1570 1580 1590 1600
PREYKAVLER EAAKKEEAKR LQYPKAFMPG NPIRQQIEET NAQIADVEDT
1610 1620 1630 1640 1650
LGATVKKSAP LDKLRGFMKY QRRSEHYRNP LKRTNDWKEL SVRLREDELR
1660 1670 1680 1690 1700
VQTARCMDCG TPFCQSDYGC PISNKIFTWN DLVFKQQWKE ALTQLLLTNN
1710 1720 1730 1740 1750
FPEFTGRVCP APCEGACTLG IIESPVGIKS VERAIIDKAW EEGWIVPRPP
1760 1770 1780 1790 1800
AERTGRRVAI IGSGPAGLAA ADQLNRAGHH VVIYERADRP GGLLQYGIPN
1810 1820 1830 1840 1850
MKLDKKVVER RIQLMIDEGI EVLTNVEVGK NGDVSLDELH KVYDAVVLAS
1860 1870 1880 1890 1900
GSTVPRDLPI PNRDSKGIHF AMEFLHKNTK SLLDSELKDG NYISAKGKDV
1910 1920 1930 1940 1950
IVIGGGDTGN DCLGTSVRHG AKSVRNLELL PIPPRERAFD NPWPQYPRVF
1960 1970 1980 1990 2000
RVDYGHAEVQ AHYGQDFREY SILTKSFEKD EDGNVKGINT VRIEWTKNSK
2010 2020 2030 2040 2050
GRWIMKEIRN SEEFFPADLV ILALGFLGPE EQATAGMNVD RDARSNISTP
2060 2070 2080 2090 2100
TKSYETSVPG IYAAGDCRRG QSLVVWGIQE GRQCAREIDL KFQGKTFLPG
2110
DGGLVKRTVN C
Length:2,111
Mass (Da):232,849
Last modified:June 1, 2001 - v1
Checksum:iD3CE58815CC4E158
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2067 – 20693CRR → SA in BAA13827 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC36924.1.
D89165 mRNA. Translation: BAA13827.1.
PIRiT42527.
RefSeqiNP_594133.1. NM_001019557.2.

Genome annotation databases

EnsemblFungiiSPAPB1E7.07.1; SPAPB1E7.07.1:pep; SPAPB1E7.07.
GeneIDi2543509.
KEGGispo:SPAPB1E7.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC36924.1.
D89165 mRNA. Translation: BAA13827.1.
PIRiT42527.
RefSeqiNP_594133.1. NM_001019557.2.

3D structure databases

ProteinModelPortaliQ9C102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279927. 1 interaction.
MINTiMINT-4702166.

Proteomic databases

MaxQBiQ9C102.
PRIDEiQ9C102.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAPB1E7.07.1; SPAPB1E7.07.1:pep; SPAPB1E7.07.
GeneIDi2543509.
KEGGispo:SPAPB1E7.07.

Organism-specific databases

EuPathDBiFungiDB:SPAPB1E7.07.
PomBaseiSPAPB1E7.07. glt1.

Phylogenomic databases

HOGENOMiHOG000031559.
InParanoidiQ9C102.
KOiK00264.
OMAiHIAMLIG.
OrthoDBiEOG7TN012.
PhylomeDBiQ9C102.

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00690.

Miscellaneous databases

PROiQ9C102.

Family and domain databases

Gene3Di2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.50.50.60. 3 hits.
3.60.20.10. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR028261. DPD_II.
IPR023753. FAD/NAD-binding_dom.
IPR017932. GATase_2_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR012220. Glu_synth_euk.
IPR002932. Glu_synthdom.
IPR006005. Glut_synth_ssu1.
IPR009051. Helical_ferredxn.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF14691. Fer4_20. 1 hit.
PF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000187. GOGAT. 1 hit.
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
TIGRFAMsiTIGR01317. GOGAT_sm_gam. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1923-2111.
    Strain: PR745.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLT1_SCHPO
AccessioniPrimary (citable) accession number: Q9C102
Secondary accession number(s): P78816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.