Reviewed, UniProtKB/Swiss-Prot Q12680 (GLT1_YEAST)

Names and origin

Protein names

Recommended name:
    Glutamate synthase [NADH]
    EC=1.4.1.14
Alternative name(s):
    NADH-GOGAT

Gene names

Name:	GLT1
Ordered Locus Names:	YDL171C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	2145 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Catalytic activity	2 L-glutamate + NAD(+) = L-glutamine + 2-oxoglutarate + NADH.
Cofactor	Binds 1 3Fe-4S cluster. FAD. FMN.
Enzyme regulation	Inhibited by homocysteine sulfonamide.
Pathway	Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADH route): step 1/1. Energy metabolism; nitrogen metabolism.
Subunit structure	Homotrimer.
Miscellaneous	Present with 18900 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the glutamate synthase family. Contains 1 glutamine amidotransferase type-2 domain.
Biophysicochemical properties	Kinetic parameters: KM=280 µM for L-glutamine KM=40 µM for 2-oxoglutarate KM=7 µM for NADH pH dependence: Optimum pH is 7-7.5. Active from pH 6 to 9.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Glutamate biosynthesis
Domain	Coiled coil Glutamine amidotransferase
Ligand	3Fe-4S FAD FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ammonia assimilation cycle Inferred from expression pattern. Source: SGD glutamate biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: SGD
Molecular function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro FMN binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro glutamate synthase (NADH) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 53	53			PRO_0000011612
	Chain	54 – 2145	2092	Glutamate synthase [NADH]		PRO_0000011613
Regions
	Domain	54 – 455	402	Glutamine amidotransferase type-2
	Nucleotide binding	1132 – 1189	58	FMN By similarity
	Nucleotide binding	1928 – 1942	15	NAD Potential
	Coiled coil	1551 – 1600	50	Potential
Sites
	Active site	54	1	For GATase activity By similarity
	Metal binding	1185	1	Iron-sulfur (3Fe-4S) By similarity
	Metal binding	1191	1	Iron-sulfur (3Fe-4S) By similarity
	Metal binding	1196	1	Iron-sulfur (3Fe-4S) By similarity
Experimental info
	Sequence conflict	166 – 173	8	NVPVDSTI → TSRRFYY in CAA61505. Ref.1
	Sequence conflict	450 – 452	3	FLV → IPS in CAA61505. Ref.1
	Sequence conflict	1753	1	V → L in CAA61505. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q12680-1 [UniParc]. Last modified September 5, 2006. Version 2. Checksum: 78184877D2167A0D	FASTA	2,145	238,102
	10 20 30 40 50 60 MPVLKSDNFD PLEEAYEGGT IQNYNDEHHL HKSWANVIPD KRGLYDPDYE HDACGVGFVA 70 80 90 100 110 120 NKHGEQSHKI VTDARYLLVN MTHRGAVSSD GNGDGAGILL GIPHEFMKRE FKLDLDLDIP 130 140 150 160 170 180 EMGKYAVGNV FFKKNEKNNK KNLIKCQKIF EDLAASFNLS VLGWRNVPVD STILGDVALS 190 200 210 220 230 240 REPTILQPLL VPLYDEKQPE FNETKFRTQL YLLRKEASLQ IGLENWFYVC SLNNTTIVYK 250 260 270 280 290 300 GQLTPAQVYN YYPDLTNAHF KSHMALVHSR FSTNTFPSWD RAQPLRWLAH NGEINTLRGN 310 320 330 340 350 360 KNWMRSREGV MNSATFKDEL DKLYPIIEEG GSDSAALDNV LELLTINGTL SLPEAVMMMV 370 380 390 400 410 420 PEAYHKDMDS DLKAWYDWAA CLMEPWDGPA LLTFTDGRYC GAILDRNGLR PCRYYITSDD 430 440 450 460 470 480 RVICASEVGV IPIENSLVVQ KGKLKPGDLF LVDTQLGEMV DTKKLKSQIS KRQDFKSWLS 490 500 510 520 530 540 KVIKLDDLLS KTANLVPKEF ISQDSLSLKV QSDPRLLANG YTFEQVTFLL TPMALTGKEA 550 560 570 580 590 600 LGSMGNDAPL ACLNENPVLL YDYFRQLFAQ VTNPPIDPIR EANVMSLECY VGPQGNLLEM 610 620 630 640 650 660 HSSQCDRLLL KSPILHWNEF QALKNIEAAY PSWSVAEIDI TFDKSEGLLG YTDTIDKITK 670 680 690 700 710 720 LASEAIDDGK KILIITDRKM GANRVSISSL IAISCIHHHL IRNKQRSQVA LILETGEARE 730 740 750 760 770 780 IHHFCVLLGY GCDGVYPYLA METLVRMNRE GLLRNVNNDN DTLEEGQILE NYKHAIDAGI 790 800 810 820 830 840 LKVMSKMGIS TLASYKGAQI FEALGLDNSI VDLCFTGTSS RIRGVTFEYL AQDAFSLHER 850 860 870 880 890 900 GYPSRQTISK SVNLPESGEY HFRDGGYKHV NEPTAIASLQ DTVRNKNDVS WQLYVKKEME 910 920 930 940 950 960 AIRDCTLRGL LELDFENSVS IPLEQVEPWT EIARRFASGA MSYGSISMEA HSTLAIAMNR 970 980 990 1000 1010 1020 LGAKSNCGEG GEDAERSAVQ ENGDTMRSAI KQVASARFGV TSYYLSDADE IQIKIAQGAK 1030 1040 1050 1060 1070 1080 PGEGGELPAH KVSKDIAKTR HSTPNVGLIS PPPHHDIYSI EDLKQLIYDL KCANPRAGIS 1090 1100 1110 1120 1130 1140 VKLVSEVGVG IVASGVAKAK ADHILVSGHD GGTGAARWTS VKYAGLPWEL GLAETHQTLV 1150 1160 1170 1180 1190 1200 LNDLRRNVVV QTDGQLRTGF DIAVAVLLGA ESFTLATVPL IAMGCVMLRR CHLNSCAVGI 1210 1220 1230 1240 1250 1260 ATQDPYLRSK FKGQPEHVIN FFYYLIQDLR QIMAKLGFRT IDEMVGHSEK LKKRDDVNAK 1270 1280 1290 1300 1310 1320 AINIDLSPIL TPAHVIRPGV PTKFTKKQDH KLHTRLDNKL IDEAEVTLDR GLPVNIDASI 1330 1340 1350 1360 1370 1380 INTDRALGST LSYRVSKKFG EDGLPKDTVV VNIEGSAGQS FGAFLASGIT FILNGDANDY 1390 1400 1410 1420 1430 1440 VGKGLSGGII VIKPPKDSKF KSDENVIVGN TCFYGATSGT AFISGSAGER FGVRNSGATI 1450 1460 1470 1480 1490 1500 VVERIKGNNA FEYMTGGRAI VLSQMESLNA FSGATGGIAY CLTSDYDDFV GKINKDTVEL 1510 1520 1530 1540 1550 1560 ESLCDPVEIA FVKNLIQEHW NYTQSDLAAR ILGNFNHYLK DFVKVIPTDY KKVLLKEKAE 1570 1580 1590 1600 1610 1620 AAKAKAKATS EYLKKFRSNQ EVDDEVNTLL IANQKAKEQE KKKSITISNK ATLKEPKVVD 1630 1640 1650 1660 1670 1680 LEDAVPDSKQ LEKNSERIEK TRGFMIHKRR HETHRDPRTR VNDWKEFTNP ITKKDAKYQT 1690 1700 1710 1720 1730 1740 ARCMDCGTPF CLSDTGCPLS NIIPKFNELL FKNQWKLALD KLLETNNFPE FTGRVCPAPC 1750 1760 1770 1780 1790 1800 EGACTLGIIE DPVGIKSVER IIIDNAFKEG WIKPCPPSTR TGFTVGVIGS GPAGLACADM 1810 1820 1830 1840 1850 1860 LNRAGHTVTV YERSDRCGGL LMYGIPNMKL DKAIVQRRID LLSAEGIDFV TNTEIGKTIS 1870 1880 1890 1900 1910 1920 MDELKNKHNA VVYAIGSTIP RDLPIKGREL KNIDFAMQLL ESNTKALLNK DLEIIREKIQ 1930 1940 1950 1960 1970 1980 GKKVIVVGGG DTGNDCLGTS VRHGAASVLN FELLPEPPVE RAKDNPWPQW PRVMRVDYGH 1990 2000 2010 2020 2030 2040 AEVKEHYGRD PREYCILSKE FIGNDEGEVT AIRTVRVEWK KSQSGVWQMV EIPNSEEIFE 2050 2060 2070 2080 2090 2100 ADIILLSMGF VGPELINGND NEVKKTRRGT IATLDDSSYS IDGGKTFACG DCRRGQSLIV 2110 2120 2130 2140 WAIQEGRKCA ASVDKFLMDG TTYLPSNGGI VQRDYKLLKE LASQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain structure of yeast glutamate synthase." Filetici P., Martegani M.P., Valenzuela L., Gonzalez A., Ballario P. Yeast 12:1359-1366(1996) [PubMed: 8923741] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96744 / CN36.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Saccharomyces cerevisiae has a single glutamate synthase gene coding for a plant-like high-molecular-weight polypeptide." Cogoni C., Valenzuela L., Gonzalez-Halphen D., Olivera H., Macino G., Ballario P., Gonzalez A. J. Bacteriol. 177:792-798(1995) [PubMed: 7836314] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-61, SUBUNIT. Strain: ATCC 96744 / CN36.
[4]	"Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae." Roon R.J., Even H.L., Larimore F. J. Bacteriol. 118:89-95(1974) [PubMed: 4362465] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
[5]	"Inhibition of homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae." Masters D.S. Jr., Meister A. J. Biol. Chem. 257:8711-8715(1982) [PubMed: 7047525] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X89221 Genomic DNA. Translation: CAA61505.1. Z67750 Genomic DNA. Translation: CAA91574.1. Z74219 Genomic DNA. Translation: CAA98745.1.
PIR	S61041.
RefSeq	NP_010110.1.
3D structure databases
HSSP	HSSP built from PDB template 1LM1 based on UniProtKB P55038.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6490N.
Proteomic databases
PeptideAtlas	Q12680.
Genome annotation databases
Ensembl	YDL171C. Saccharomyces cerevisiae. [Contig view]
GeneID	851383.
GenomeReviews	Gene locus YDL171C in contig Z71256_GR.
KEGG	sce:YDL171C.
NMPDR	fig|4932.3.peg.844.
Organism-specific databases
CYGD	YDL171c.
SGD	S000002330. GLT1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q12680.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13146.
Gene expression databases
ArrayExpress	Q12680.
GermOnline	YDL171C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000759. Adrndx_reductase. IPR013785. Aldolase_TIM. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR012285. Fum_reductase_C. IPR000583. GATase_2. IPR002932. Glu_synth_centr_C. IPR006982. Glu_synth_centr_N. IPR002489. Glu_synthase_C. IPR006005. Glut_synth_sub1. IPR012220. GOGAT_euk. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 2 hits. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit. G3DSA:2.160.20.60. Glu_synthase_C. 1 hit.
Pfam	PF00310. GATase_2. 1 hit. PF04898. Glu_syn_central. 1 hit. PF01645. Glu_synthase. 1 hit. PF01493. GXGXG. 1 hit. PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PIRSF	PIRSF000187. GOGAT. 1 hit.
PRINTS	PR00419. ADXRDTASE. PR00368. FADPNR.
TIGRFAMs	TIGR01317. GOGAT_sm_gam. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	Q12680.
NextBio	968525.

Entry information

Entry name

GLT1_YEAST

Accession

Primary (citable) accession number: Q12680
Secondary accession number(s): Q12290

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 5, 2006
Last modified:	November 25, 2008
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)