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Protein

Glutamate synthase [NADH], amyloplastic

Gene
N/A
Organism
Medicago sativa (Alfalfa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the assimilation of symbiotically fixed nitrogen into amino acids in root nodules.2 Publications

Catalytic activityi

2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by malate, citrate, glutamate, NAD+ and azaserine, but not by 2-2' dipyridil and N-ethylmaleimide.1 Publication

Kineticsi

  1. KM=466 µM for glutamine1 Publication
  2. KM=33 µM for 2-oxoglutarate1 Publication
  3. KM=4.2 µM for NADH1 Publication

    pH dependencei

    Optimum pH is 7.5-8.5.1 Publication

    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. Glutamate synthase [NADH], amyloplastic
    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 sitei102 – 1021NucleophilePROSITE-ProRule annotation
    Metal bindingi1246 – 12461Iron-sulfur (3Fe-4S)By similarity
    Metal bindingi1252 – 12521Iron-sulfur (3Fe-4S)By similarity
    Metal bindingi1257 – 12571Iron-sulfur (3Fe-4S)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1193 – 125058FMNBy similarityAdd
    BLAST
    Nucleotide bindingi1974 – 198815NADSequence analysisAdd
    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, NAD

    Enzyme and pathway databases

    UniPathwayiUPA00045.
    UPA00634; UER00690.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate synthase [NADH], amyloplastic (EC:1.4.1.14)
    Alternative name(s):
    NADH-GOGAT
    OrganismiMedicago sativa (Alfalfa)
    Taxonomic identifieri3879 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Amyloplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 101101Amyloplast1 PublicationAdd
    BLAST
    Chaini102 – 21942093Glutamate synthase [NADH], amyloplasticPRO_0000011617Add
    BLAST

    Expressioni

    Tissue specificityi

    Expressed in infected cells in root nodules. Barely detected in roots and stems.4 Publications

    Inductioni

    Up-regulated during nodule development.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ03460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini102 – 503402Glutamine 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, Transit peptide

    Family and domain databases

    Gene3Di2.160.20.60. 1 hit.
    3.20.20.70. 2 hits.
    3.40.50.720. 2 hits.
    3.50.50.60. 1 hit.
    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.
    IPR016040. NAD(P)-bd_dom.
    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.
    SSF51905. SSF51905. 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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q03460-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNSLSLTFT ALNNPQINAI SNPNARLRPL ARVTRCSATC VERKRWLGTK
    60 70 80 90 100
    LRSGGGLERI QLWESGGLGR LPKLRVAVKS SFSAVPDKPM GLYDPAFDKD
    110 120 130 140 150
    SCGVGFVAEL NGQSSRKTVT DALEMLVRMT HRGACGCEAN TGDGAGILVA
    160 170 180 190 200
    LPHGFYQEVV DFQLPPQGNY AVGMFFLPKS DSRRKESKNI FTKVAESLGH
    210 220 230 240 250
    KVLGWRSVPT DNTGLGKSAQ LTEPVIEQVF LTPSSDSKVD LEKQMYILRK
    260 270 280 290 300
    LSMVSITSAL NLQSDGITDF YICSLSSRTV IYKGQLTPAQ LGEYYYADLG
    310 320 330 340 350
    NERFTSYMAL IHSRFSTNTF PSWDRAQPFR VLGHNGEINT LRGNVNWIKA
    360 370 380 390 400
    REGLLKCKEL GLSENDLKKF LPIVDANSSD SGCFDGVLEF LLHSGKSLPE
    410 420 430 440 450
    AVMMMIPEAW QNDKNMDPQR KAFYEYYSAL MEPWDGPALI SFTDGHYLGA
    460 470 480 490 500
    TLDRNGLRPG RFYVTHSGRV IMASEVGVVD IPPEDVCRKG RLNPGMMLLV
    510 520 530 540 550
    DFEKQIVVND DALKEQYSLA RPYGDWLEKQ KIELKDIIDS VHESDIVPPT
    560 570 580 590 600
    ISGVPPLSND DVDMENMGIQ GLLAPLKAFG YSVESLEILL LPMAKDGVEA
    610 620 630 640 650
    LGSMGNDTPL AVMSNREKLT FEYFKQMFAQ VTNPPIDPIR EKIVTSMRCM
    660 670 680 690 700
    VGPEGDLTET TEEQCHRLSL KGPLLSTKEM EAIKKMNYRG WRSKVIDITY
    710 720 730 740 750
    SKERGTKGLE EALDRICTEA HNAISEGYTT LVLSDRAFSK KHVAVSSLLA
    760 770 780 790 800
    VGAVHQHLVK TLERTRVALM VESAEPREVH HFCTLVGFGA DAICPYLAIE
    810 820 830 840 850
    AIWRLQVDGK IPPKASGDFN SKDELVKKYF KASTYGMMKV LAKMGISTLA
    860 870 880 890 900
    SYKGAQIFEA LGLSSEVIEK CFAGTPSRVE GATFEMLAQD ALHLHELAFP
    910 920 930 940 950
    SRIFSPGSAE AVALPNPGDY HWRKGGEVHL NDPLAIAKLQ EAARTNSVDA
    960 970 980 990 1000
    YKQYSKTIHE LNKACNLRGL LKFKDAASKV PISEVEPASE IVKRFCTGAM
    1010 1020 1030 1040 1050
    SYGSISLEAH TALATAMNTI GGKSNTGEGG EQPSRMEPLA DGSRNPKRSA
    1060 1070 1080 1090 1100
    IKQVASGRFG VSSYYLTNAD ELQIKMAQGA KPGEGGELPG HKVIGDIAIT
    1110 1120 1130 1140 1150
    RNSTAGVGLI SPPPHHDIYS IEDLAQLIHD LKNANPAARI SVKLVSEAGV
    1160 1170 1180 1190 1200
    GVIASGVVKG HAEHVLISGH DGGTGASRWT GIKSAGLPWE LGLAETHQTL
    1210 1220 1230 1240 1250
    VANDLRGRTT LQTDGQLKTG RDVAIAALLG AEEYGFSTAP LITLGCIMMR
    1260 1270 1280 1290 1300
    KCHKNTCPVG IATQDPVLRE KFAGEPEHVI NFFFMVAEEM REIMSQLGFR
    1310 1320 1330 1340 1350
    TVNEMVGRSD MLEVDKEVVK GNAKLENIDL SLLLRPAAEL RPEAAQYCVQ
    1360 1370 1380 1390 1400
    KQDHGLDMAL DNKLISLSNA ALEKGLPVYI ETPICNTNRA VGTMLSHEVT
    1410 1420 1430 1440 1450
    KRYNLAGLPA DTIHIQFTGS AGQSFGAFLC PGITLELEGD SNDYIGKGLS
    1460 1470 1480 1490 1500
    GGKVVVYPPK GSNFDPKDNI LIGNVALYGA TRGEAYFNGM AAERFCVRNS
    1510 1520 1530 1540 1550
    GALAVVEGVG DHGCEYMTGG TVVVLGKTGR NFAAGMSGGI AYVLDVDGTF
    1560 1570 1580 1590 1600
    QSRCNLELVD LDKVEEEEDI ITLRMLIQQH QRHTNSLLAK EVLVDFENLL
    1610 1620 1630 1640 1650
    PKFVKVFPRE YKRVLASMKS DAASKDAVER AAEDVDEQDD EAQAVEKDAF
    1660 1670 1680 1690 1700
    EELKKLATAS LNEKPSEAPK RPSQVTDAVK HRGFVAYERE GVQYRDPNVR
    1710 1720 1730 1740 1750
    LNDWNEVMME TKPGPLLKTQ SARCMDCGTP FCHQENSGCP LGNKIPEFNE
    1760 1770 1780 1790 1800
    LVYQNRWQEA LERLLETNNF PEFTGRVCPA PCEGSCVLGI IENPVSIKNI
    1810 1820 1830 1840 1850
    ECAIIDKAFE EGWMIPRPPV KRTGKRVAIV GSGPSGLAAA DQLNKMGHIV
    1860 1870 1880 1890 1900
    TVFERADRIG GLMMYGVPNM KTDKVDIVQR RVNLMAEEGI NFVVNANIGL
    1910 1920 1930 1940 1950
    DPLYSLERLR EENDAIVLAV GATKPRDLPV PGRELSGVHF AMEFLHANTK
    1960 1970 1980 1990 2000
    SLLDSNLQDG NYISAKGKKV VVIGGGDTGT DCIGTSIRHG CTAVVNLELL
    2010 2020 2030 2040 2050
    PQPPPTRAPG NPWPQWPRIF RVDYGHQEAE TKFGKDPRTY EVLTKRFVGD
    2060 2070 2080 2090 2100
    ENGVVKGLEV VRVCWEKDET GKFQFKEIEG SEEIIEADLV LLAMGFLGPE
    2110 2120 2130 2140 2150
    ATIAEKLGVE RDNRSNFKAD YGRFSTSVDG VFAAGDCRRG QSLVVWAISE
    2160 2170 2180 2190
    GRQAAAQVDS YLTNEDHGID GNQDEFVKRQ QDLNKKHSKH TVMT
    Length:2,194
    Mass (Da):240,374
    Last modified:October 1, 1993 - v1
    Checksum:i370A1B0F178367C4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331V → F in AAB41904 (PubMed:7550373).Curated
    Sequence conflicti57 – 571L → P in AAB41904 (PubMed:7550373).Curated
    Sequence conflicti185 – 1851K → M in AAB41904 (PubMed:7550373).Curated
    Sequence conflicti742 – 7421H → R in AAB41904 (PubMed:7550373).Curated
    Sequence conflicti989 – 9891S → G in AAB41904 (PubMed:7550373).Curated
    Sequence conflicti1503 – 15031L → Q in AAB41904 (PubMed:7550373).Curated
    Sequence conflicti2154 – 21541A → R in AAB41904 (PubMed:7550373).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L01660 mRNA. Translation: AAB46617.1.
    L37606 Genomic DNA. Translation: AAB41904.1.
    PIRiJQ1977.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L01660 mRNA. Translation: AAB46617.1.
    L37606 Genomic DNA. Translation: AAB41904.1.
    PIRiJQ1977.

    3D structure databases

    ProteinModelPortaliQ03460.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00045.
    UPA00634; UER00690.

    Family and domain databases

    Gene3Di2.160.20.60. 1 hit.
    3.20.20.70. 2 hits.
    3.40.50.720. 2 hits.
    3.50.50.60. 1 hit.
    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.
    IPR016040. NAD(P)-bd_dom.
    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.
    SSF51905. SSF51905. 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...

    Entry informationi

    Entry nameiGLSN_MEDSA
    AccessioniPrimary (citable) accession number: Q03460
    Secondary accession number(s): Q40360
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: December 9, 2015
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. 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.