ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q03460

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GLSN_MEDSA
Primary accession number Q03460
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Glutamate synthase [NADH], amyloplastic [Precursor]
Synonyms EC 1.4.1.14
NADH-GOGAT
Gene name None
From
Medicago sativa (Alfalfa) [TaxID: 3879] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Trifolieae; Medicago.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 102-114.
DOI=10.1105/tpc.5.2.215; PubMed=8453303 [NCBI, ExPASy, EBI, Israel, Japan]
Gregerson R.G., Miller S.S., Twary S.N., Gantt J.S., Vance C.P.;
"Molecular characterization of NADH-dependent glutamate synthase from alfalfa nodules.";
Plant Cell 5:215-226(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L01660; AAB46617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ1977; JQ1977.
3D structure databases
HSSP P55038; 1LM1. [HSSP ENTRY / PDB]
ModBase Q03460.
Ontologies
GO
GO:0009501; Cellular component: amyloplast (inferred from electronic annotation from UniProtKB-KW).
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0051538; Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0010181; Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0016040; Molecular function: glutamate synthase (NADH) activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0006537; Biological process: glutamate biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006541; Biological process: glutamine metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
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.
IPR016040; NAD(P)-bd.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 2.
G3DSA:1.10.1060.10; Fum_reductase_C; 1.
G3DSA:2.160.20.60; Glu_synthase_C; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00310; GATase_2; 1.
PF04898; Glu_syn_central; 1.
PF01645; Glu_synthase; 1.
PF01493; GXGXG; 1.
PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000187; GOGAT; 1.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00411; PNDRDTASEI.
TIGRFAMs TIGR01317; GOGAT_sm_gam; 1.
PROSITE PS51278; GATASE_TYPE_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q03460.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3Fe-4S; Amino-acid biosynthesis; Amyloplast; Direct protein sequencing; FAD; Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
TRANSIT   1    101  101     Amyloplast. 
CHAIN   102   2194  2093     Glutamate synthase [NADH], amyloplastic. PRO_0000011617
DOMAIN   102    503  402     Glutamine amidotransferase type-2. 
NP_BIND   1193   1250  58     FMN (By similarity). 
NP_BIND   1974   1988  15     NAD (Potential). 
ACT_SITE   102    102        For GATase activity (By similarity). 
METAL   1246   1246        Iron-sulfur (3Fe-4S) (By similarity). 
METAL   1252   1252        Iron-sulfur (3Fe-4S) (By similarity). 
METAL   1257   1257        Iron-sulfur (3Fe-4S) (By similarity). 
Sequence information
Length: 2194 AA [This is the length of the unprocessed precursor] Molecular weight: 240374 Da [This is the MW of the unprocessed precursor] CRC64: 370A1B0F178367C4 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSNSLSLTFT ALNNPQINAI SNPNARLRPL ARVTRCSATC VERKRWLGTK LRSGGGLERI 

        70         80         90        100        110        120 
QLWESGGLGR LPKLRVAVKS SFSAVPDKPM GLYDPAFDKD SCGVGFVAEL NGQSSRKTVT 

       130        140        150        160        170        180 
DALEMLVRMT HRGACGCEAN TGDGAGILVA LPHGFYQEVV DFQLPPQGNY AVGMFFLPKS 

       190        200        210        220        230        240 
DSRRKESKNI FTKVAESLGH KVLGWRSVPT DNTGLGKSAQ LTEPVIEQVF LTPSSDSKVD 

       250        260        270        280        290        300 
LEKQMYILRK LSMVSITSAL NLQSDGITDF YICSLSSRTV IYKGQLTPAQ LGEYYYADLG 

       310        320        330        340        350        360 
NERFTSYMAL IHSRFSTNTF PSWDRAQPFR VLGHNGEINT LRGNVNWIKA REGLLKCKEL 

       370        380        390        400        410        420 
GLSENDLKKF LPIVDANSSD SGCFDGVLEF LLHSGKSLPE AVMMMIPEAW QNDKNMDPQR 

       430        440        450        460        470        480 
KAFYEYYSAL MEPWDGPALI SFTDGHYLGA TLDRNGLRPG RFYVTHSGRV IMASEVGVVD 

       490        500        510        520        530        540 
IPPEDVCRKG RLNPGMMLLV DFEKQIVVND DALKEQYSLA RPYGDWLEKQ KIELKDIIDS 

       550        560        570        580        590        600 
VHESDIVPPT ISGVPPLSND DVDMENMGIQ GLLAPLKAFG YSVESLEILL LPMAKDGVEA 

       610        620        630        640        650        660 
LGSMGNDTPL AVMSNREKLT FEYFKQMFAQ VTNPPIDPIR EKIVTSMRCM VGPEGDLTET 

       670        680        690        700        710        720 
TEEQCHRLSL KGPLLSTKEM EAIKKMNYRG WRSKVIDITY SKERGTKGLE EALDRICTEA 

       730        740        750        760        770        780 
HNAISEGYTT LVLSDRAFSK KHVAVSSLLA VGAVHQHLVK TLERTRVALM VESAEPREVH 

       790        800        810        820        830        840 
HFCTLVGFGA DAICPYLAIE AIWRLQVDGK IPPKASGDFN SKDELVKKYF KASTYGMMKV 

       850        860        870        880        890        900 
LAKMGISTLA SYKGAQIFEA LGLSSEVIEK CFAGTPSRVE GATFEMLAQD ALHLHELAFP 

       910        920        930        940        950        960 
SRIFSPGSAE AVALPNPGDY HWRKGGEVHL NDPLAIAKLQ EAARTNSVDA YKQYSKTIHE 

       970        980        990       1000       1010       1020 
LNKACNLRGL LKFKDAASKV PISEVEPASE IVKRFCTGAM SYGSISLEAH TALATAMNTI 

      1030       1040       1050       1060       1070       1080 
GGKSNTGEGG EQPSRMEPLA DGSRNPKRSA IKQVASGRFG VSSYYLTNAD ELQIKMAQGA 

      1090       1100       1110       1120       1130       1140 
KPGEGGELPG HKVIGDIAIT RNSTAGVGLI SPPPHHDIYS IEDLAQLIHD LKNANPAARI 

      1150       1160       1170       1180       1190       1200 
SVKLVSEAGV GVIASGVVKG HAEHVLISGH DGGTGASRWT GIKSAGLPWE LGLAETHQTL 

      1210       1220       1230       1240       1250       1260 
VANDLRGRTT LQTDGQLKTG RDVAIAALLG AEEYGFSTAP LITLGCIMMR KCHKNTCPVG 

      1270       1280       1290       1300       1310       1320 
IATQDPVLRE KFAGEPEHVI NFFFMVAEEM REIMSQLGFR TVNEMVGRSD MLEVDKEVVK 

      1330       1340       1350       1360       1370       1380 
GNAKLENIDL SLLLRPAAEL RPEAAQYCVQ KQDHGLDMAL DNKLISLSNA ALEKGLPVYI 

      1390       1400       1410       1420       1430       1440 
ETPICNTNRA VGTMLSHEVT KRYNLAGLPA DTIHIQFTGS AGQSFGAFLC PGITLELEGD 

      1450       1460       1470       1480       1490       1500 
SNDYIGKGLS GGKVVVYPPK GSNFDPKDNI LIGNVALYGA TRGEAYFNGM AAERFCVRNS 

      1510       1520       1530       1540       1550       1560 
GALAVVEGVG DHGCEYMTGG TVVVLGKTGR NFAAGMSGGI AYVLDVDGTF QSRCNLELVD 

      1570       1580       1590       1600       1610       1620 
LDKVEEEEDI ITLRMLIQQH QRHTNSLLAK EVLVDFENLL PKFVKVFPRE YKRVLASMKS 

      1630       1640       1650       1660       1670       1680 
DAASKDAVER AAEDVDEQDD EAQAVEKDAF EELKKLATAS LNEKPSEAPK RPSQVTDAVK 

      1690       1700       1710       1720       1730       1740 
HRGFVAYERE GVQYRDPNVR LNDWNEVMME TKPGPLLKTQ SARCMDCGTP FCHQENSGCP 

      1750       1760       1770       1780       1790       1800 
LGNKIPEFNE LVYQNRWQEA LERLLETNNF PEFTGRVCPA PCEGSCVLGI IENPVSIKNI 

      1810       1820       1830       1840       1850       1860 
ECAIIDKAFE EGWMIPRPPV KRTGKRVAIV GSGPSGLAAA DQLNKMGHIV TVFERADRIG 

      1870       1880       1890       1900       1910       1920 
GLMMYGVPNM KTDKVDIVQR RVNLMAEEGI NFVVNANIGL DPLYSLERLR EENDAIVLAV 

      1930       1940       1950       1960       1970       1980 
GATKPRDLPV PGRELSGVHF AMEFLHANTK SLLDSNLQDG NYISAKGKKV VVIGGGDTGT 

      1990       2000       2010       2020       2030       2040 
DCIGTSIRHG CTAVVNLELL PQPPPTRAPG NPWPQWPRIF RVDYGHQEAE TKFGKDPRTY 

      2050       2060       2070       2080       2090       2100 
EVLTKRFVGD ENGVVKGLEV VRVCWEKDET GKFQFKEIEG SEEIIEADLV LLAMGFLGPE 

      2110       2120       2130       2140       2150       2160 
ATIAEKLGVE RDNRSNFKAD YGRFSTSVDG VFAAGDCRRG QSLVVWAISE GRQAAAQVDS 

      2170       2180       2190 
YLTNEDHGID GNQDEFVKRQ QDLNKKHSKH TVMT
Q03460 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!