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Reviewed, UniProtKB/Swiss-Prot Q05755 (GLTB_AZOBR)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Glutamate synthase [NADPH] large chain
    EC=1.4.1.13
Alternative name(s):
    Glutamate synthase subunit alpha
      Short name=GLTS alpha chain
    NADPH-GOGAT
Gene names
Name: gltB
OrganismAzospirillum brasilense
Taxonomic identifier192 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Azospirillum

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Protein attributes

Sequence length1515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

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 (NADPH route): step 1/1.

Energy metabolism; nitrogen metabolism.

Subunit structure

Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit.

Miscellaneous

Glutamine binds to the large subunit and transfers the amido group to 2-oxo-glutamate that apparently binds to the small subunit.

Sequence similarities

Belongs to the glutamate synthase family.

Contains 1 glutamine amidotransferase type-2 domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 3636 Ref.1
PRO_0000011618
Chain37 – 15151479Glutamate synthase [NADPH] large chain
PRO_0000011619

Regions

Domain37 – 432396Glutamine amidotransferase type-2
Nucleotide binding1085 – 114258FMN By similarity
Nucleotide binding1086 – 114257FMN By similarity

Sites

Active site371For GATase activity By similarity
Metal binding11381Iron-sulfur (3Fe-4S) By similarity
Metal binding11441Iron-sulfur (3Fe-4S) By similarity
Metal binding11491Iron-sulfur (3Fe-4S) By similarity

Secondary structure

1 ....................................................................................................................................................................................................................................................................... 1515
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q05755-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: ED913218DBFCEE92

FASTA1,515166,018
        10         20         30         40         50         60 
MTTELNQGEQ FVADFRANAA ALTTANAYNP EDEHDACGVG FIAAIDGKPR RSVVEKGIEA 

        70         80         90        100        110        120 
LKAVWHRGAV DADGKTGDGA GIHVAVPQKF FKDHVKVIGH RAPDNKLAVG QVFLPRISLD 

       130        140        150        160        170        180 
AQEACRCIVE TEILAFGYYI YGWRQVPINV DIIGEKANAT RPEIEQIIVG NNKGVSDEQF 

       190        200        210        220        230        240 
ELDLYIIRRR IEKAVKGEQI NDFYICSLSA RSIIYKGMFL AEQLTTFYPD LLDERFESDF 

       250        260        270        280        290        300 
AIYHQRYSTN TFPTWPLAQP FRMLAHNGEI NTVKGNVNWM KAHETRMEHP AFGTHMQDLK 

       310        320        330        340        350        360 
PVIGVGLSDS GSLDTVFEVM VRAGRTAPMV KMMLVPQALT SSQTTPDNHK ALIQYCNSVM 

       370        380        390        400        410        420 
EPWDGPAALA MTDGRWVVGG MDRNGLRPMR YTITTDGLII GGSETGMVKI DETQVIEKGR 

       430        440        450        460        470        480 
LGPGEMIAVD LQSGKLYRDR ELKDHLATLK PWDKWVQNTT HLDELVKTAS LKGEPSDMDK 

       490        500        510        520        530        540 
AELRRRQQAF GLTMEDMELI LHPMVEDGKE AIGSMGDDSP IAVLSDKYRG LHHFFRQNFS 

       550        560        570        580        590        600 
QVTNPPIDSL RERRVMSLKT RLGNLGNILD EDETQTRLLQ LESPVLTTAE FRAMRDYMGD 

       610        620        630        640        650        660 
TAAEIDATFP VDGGPEALRD ALRRIRQETE DAVRGGATHV ILTDEAMGPA RAAIPAILAT 

       670        680        690        700        710        720 
GAVHTHLIRS NLRTFTSLNV RTAEGLDTHY FAVLIGVGAT TVNAYLAQEA IAERHRRGLF 

       730        740        750        760        770        780 
GSMPLEKGMA NYKKAIDDGL LKIMSKMGIS VISSYRGGGN FEAIGLSRAL VAEHFPAMVS 

       790        800        810        820        830        840 
RISGIGLNGI QKKVLEQHAT AYNEEVVALP VGGFYRFRKS GDRHGWEGGV IHTLQQAVTN 

       850        860        870        880        890        900 
DSYTTFKKYS EQVNKRPPMQ LRDLLELRST KAPVPVDEVE SITAIRKRFI TPGMSMGALS 

       910        920        930        940        950        960 
PEAHGTLNVA MNRIGAKSDS GEGGEDPARF RPDKNGDNWN SAIKQVASGR FGVTAEYLNQ 

       970        980        990       1000       1010       1020 
CRELEIKVAQ GAKPGEGGQL PGFKVTEMIA RLRHSTPGVM LISPPPHHDI YSIEDLAQLI 

      1030       1040       1050       1060       1070       1080 
YDLKQINPDA KVTVKLVSRS GIGTIAAGVA KANADIILIS GNSGGTGASP QTSIKFAGLP 

      1090       1100       1110       1120       1130       1140 
WEMGLSEVHQ VLTLNRLRHR VRLRTDGGLK TGRDIVIAAM LGAEEFGIGT ASLIAMGCIM 

      1150       1160       1170       1180       1190       1200 
VRQCHSNTCP VGVCVQDDKL RQKFVGTPEK VVNLFTFLAE EVREILAGLG FRSLNEVIGR 

      1210       1220       1230       1240       1250       1260 
TDLLHQVSRG AEHLDDLDLN PRLAQVDPGE NARYCTLQGR NEVPDTLDAR IVADARPLFE 

      1270       1280       1290       1300       1310       1320 
EGEKMQLAYN ARNTQRAIGT RLSSMVTRKF GMFGLQPGHI TIRLRGTAGQ SLGAFAVQGI 

      1330       1340       1350       1360       1370       1380 
KLEVMGDAND YVGKGLSGGT IVVRPTTSSP LETNKNTIIG NTVLYGATAG KLFAAGQAGE 

      1390       1400       1410       1420       1430       1440 
RFAVRNSGAT VVVEGCGSNG CEYMTGGTAV ILGRVGDNFA AGMTGGMAYV YDLDDSLPLY 

      1450       1460       1470       1480       1490       1500 
INDESVIFQR IEVGHYESQL KHLIEEHVTE TQSRFAAEIL NDWAREVTKF WQVVPKEMLN 

      1510 
RLEVPVHLPK AISAE

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References

[1]"Glutamate synthase genes of the diazotroph Azospirillum brasilense. Cloning, sequencing, and analysis of functional domains."
Pelanda R., Vanoni M.A., Perego M., Piubelli L., Galizzi A., Curti B., Zanetti G.
J. Biol. Chem. 268:3099-3106(1993) [PubMed: 8428988] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 37-56; 778-799 AND 1325-1345.
Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.
[2]"Isolation of a glutamate synthase (GOGAT)-negative, pleiotropically N utilization-defective mutant of Azospirillum brasilense: cloning and partial characterization of GOGAT structural gene."
Mandal A.K., Ghosh S.
J. Bacteriol. 175:8024-8029(1993) [PubMed: 7902833] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 834-927.
Strain: RG.
[3]"Structural studies on the subunits of glutamate synthase from Azospirillum brasilense."
Vanoni M.A., Negri A., Zanetti G., Ronchi S., Curti B.
Biochim. Biophys. Acta 1039:374-377(1990) [PubMed: 2198943] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF192408 Genomic DNA. Translation: AAA22179.1.
X71632 Genomic DNA. Translation: CAA50639.1.
PIRB46602.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EA0X-ray3.00A/B37-1515[»]
2VDCelectron microscopy9.50A/B/C/D/E/F37-1508[»]
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-13079.
BRENDA1.4.1.13. 1315.

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...

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Entry information

Entry nameGLTB_AZOBR
AccessionPrimary (citable) accession number: Q05755
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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