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Reviewed, UniProtKB/Swiss-Prot P23225 (GLTB_MAIZE)

Last modified June 16, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ferredoxin-dependent glutamate synthase, chloroplastic
    EC=1.4.7.1
Alternative name(s):
    Fd-GOGAT
Gene names
Name: GLSF
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACCAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length1616 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+.

Cofactor

Binds 1 3Fe-4S cluster.

FAD.

FMN.

Pathway

Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin route): step 1/1.

Energy metabolism; nitrogen metabolism.

Subunit structure

Monomer.

Subcellular location

Plastidchloroplast stroma.

Tissue specificity

Mostly in green tissues and lesser in non-photosynthetic tissues.

Sequence similarities

Belongs to the glutamate synthase family.

Contains 1 glutamine amidotransferase type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 9797Chloroplast
Chain98 – 16161519Ferredoxin-dependent glutamate synthase, chloroplastic
PRO_0000011616

Regions

Domain98 – 497400Glutamine amidotransferase type-2
Nucleotide binding1176 – 123358FMN By similarity

Sites

Active site981For GATase activity By similarity
Metal binding12291Iron-sulfur (3Fe-4S) By similarity
Metal binding12351Iron-sulfur (3Fe-4S) By similarity
Metal binding12401Iron-sulfur (3Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P23225-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 67724CBFA0AEB053

FASTA1,616175,173
        10         20         30         40         50         60 
MATLPRAAPP TPAALLPLPR AAPPLLLAGR AAAARRSRLR ARGPSAAARR SWVVASAASS 

        70         80         90        100        110        120 
SSRAVVGGVA RREAPPAPQK PTQQAADLNH ILSERGACGV GFVANLKNMS SFDIVRDALM 

       130        140        150        160        170        180 
ALGCMEHRGG CGADSDSGDG AGLMSAVPWD LFDDWASKQG LALFDRRNTG VGMVFLPQDE 

       190        200        210        220        230        240 
KSMEEAKAAT EKVFVDEGLE VLGWRPVPFN VSVVGRNAKE TMPNIQQIFV KVAKEDNADD 

       250        260        270        280        290        300 
IERELYISRK LIERAAKSFS WADELYFCSL SSRTIVYKGM LRSEVLGQFY LDLQNELYKS 

       310        320        330        340        350        360 
PFAIYHRRFS TNTSPRWPLA QPMRLLGHNG EINTIQGNLN WMRSRETTLK SPVWRGREHE 

       370        380        390        400        410        420 
ICPFGDPKAS DSANLDSTAE LLLRSGRSPA EALMILVPEA YKNHPTLSIK YPEVTDFYDY 

       430        440        450        460        470        480 
YKGQMEAWDG PALLLFSDGR TVGATLDRNG LRPARYWRTS DDFVYVASEV GVIPMDESKV 

       490        500        510        520        530        540 
VMKGRLGPGM MITVDLQTGQ VLENTEVKKT VASASPYGTW LQECTRLIKP VNFLSSTIMD 

       550        560        570        580        590        600 
NETVLRHQQA FGYSSEDVQM VIESMASQGK EPTFCMGDDI PLAVLSQRPH LLYDYFKQRF 

       610        620        630        640        650        660 
AQVTNPAIDP LREGLVMSLE VNIGKRGNIL EVGPENADQV ALSSPVLNEG ELETLLNDSK 

       670        680        690        700        710        720 
LKPKVLSTYF DIRKGLDGSL DKTIQALCEE ADAAVRSGSQ LLVLSDRSEA PEPTRPAIPI 

       730        740        750        760        770        780 
LLAVGAIHQH LIQNGLRMSA SIVADTAQCF STHHFACLIG YGASAVCPYL ALETCRQWRL 

       790        800        810        820        830        840 
SNKTLNLMRN GKMPTVTIEQ AQRNFIKAVK SGLLKILSKM GISLLSSYCG AQIFEIYGLG 

       850        860        870        880        890        900 
QEVVDLAFCG SVSKIGGLTL DELGRETLSF WVKAFSEDTA KRLENFGFIQ SRPGGEYHAN 

       910        920        930        940        950        960 
NPEMSKLLHK AIREKRDNAY TVYQQHLASR PVNVLRDLLE LKSDRAPIPI GKVESATSIV 

       970        980        990       1000       1010       1020 
ERFCTGGMSL GAISRETHEA IAIAMNRIGG KSNSGEGGED PIRWNPLTDV VDGYSPTLPH 

      1030       1040       1050       1060       1070       1080 
LKGLQNGDTA TSAIKQVASG RFGVTPTFLV NADQIEIKIA QGAKPGEGGQ LPGKKVSAYI 

      1090       1100       1110       1120       1130       1140 
ARLRNSKPGV PLISPPPHHD IYSIEDLAQL IYDLHQINPK AKVSVKLVSE AGIGTVASGV 

      1150       1160       1170       1180       1190       1200 
SKANADIIQI SGHDGGTGAS PISSIKHAGG PWELGLTETN QTLIQNGLRE RVVLRVDGGF 

      1210       1220       1230       1240       1250       1260 
RSGQDVLIAA AMGADEYGFG SVAMIATGCV MARICHTNNC PVGVASQREE LRARFPGVPG 

      1270       1280       1290       1300       1310       1320 
DLVNYFLFVA EEVRAALAQL GYEKLDDIIG RTDLLKPKHI SLVKTQHIDL GYLLSNAGLP 

      1330       1340       1350       1360       1370       1380 
EWSSSQIRSQ DVHTNGPVLD ETILADPEIA DAIENEKEVS KAFQIYNVDR AVCGRVAGVI 

      1390       1400       1410       1420       1430       1440 
AKKYGDTGFA GQLNITFNGS AGQSFGCFLT PGMNIRLVGE ANDYVGKGMA GGELVVVPVD 

      1450       1460       1470       1480       1490       1500 
KTGFVPEDAT IVGNTCLYGA TGGQVFVRGK AGERFAVRNS LCQAVVEGTG DHCCEYMTGG 

      1510       1520       1530       1540       1550       1560 
CVVVLGKAGR NVAAGMTGGL AYILDEDDTL VPKVNKEIVK MQRVNAPAGQ MQLKGLIEAY 

      1570       1580       1590       1600       1610 
VEKTGSEKGI AILREWEAYL PLFWQLVPPS EEDSPEACAE FERVLAKQAT TQLSAK 

« Hide

References

[1]"Molecular cloning and characterization of complementary DNA encoding for ferredoxin-dependent glutamate synthase in maize leaf."
Sakakibara H., Watanabe M., Hase T., Sugiyama T.
J. Biol. Chem. 266:2028-2035(1991) [PubMed: 1989968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 97-109 AND 790-802.
Strain: cv. Golden cross Bantam T51.
Tissue: Leaf.

Cross-references

Sequence databases

M59190 mRNA. Translation: AAA33463.1.
PIRA38596.
RefSeqNP_001105693.1.
UniGeneZm.54067

3D structure databases

HSSPHSSP built from PDB template 1OFD based on UniProtKB P55038.
ModBaseSearch...

Genome annotation databases

GeneID542710.

Organism-specific databases

GrameneP23225.
MaizeGDB40403.

Enzyme and pathway databases

BRENDA1.4.7.1. 289.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR000583. GATase_2.
IPR017932. GATase_II.
IPR002932. Glu_synth_centr_C.
IPR006982. Glu_synth_centr_N.
IPR002489. Glu_synthase_C.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 2 hits.
G3DSA:2.160.20.60. Glu_synthase_C. 1 hit.
PfamPF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
[Graphical view]
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLTB_MAIZE
AccessionPrimary (citable) accession number: P23225
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents