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Reviewed, UniProtKB/Swiss-Prot P09831 (GLTB_ECOLI)

Last modified June 16, 2009. Version 94. 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
Synonyms: aspB
Ordered Locus Names: b3212, JW3179
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1517 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 + 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

gltDP098322EBI-551179,EBI-544293

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4242
PRO_0000011620
Chain43 – 15171475Glutamate synthase [NADPH] large chain
PRO_0000011621

Regions

Domain43 – 433391Glutamine amidotransferase type-2
Nucleotide binding1080 – 113253FMN By similarity

Sites

Active site431For GATase activity By similarity
Metal binding11331Iron-sulfur (3Fe-4S) By similarity
Metal binding11391Iron-sulfur (3Fe-4S) By similarity
Metal binding11441Iron-sulfur (3Fe-4S) By similarity

Experimental info

Sequence conflict105 – 1095GWRLA → LAFR in AAA23904. Ref.1
Sequence conflict1401E → N in AAA23904. Ref.1
Sequence conflict220 – 24021LCMPT…LRLES → CVCRRICRVLSGSCGPASGM in AAA23904. Ref.1
Sequence conflict259 – 28224LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG Ref.1
Sequence conflict259 – 28224LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG Ref.4
Sequence conflict4601N → K in AAA23904. Ref.1
Sequence conflict5741A → T in AAA23904. Ref.1
Sequence conflict8631D → H in AAA23904. Ref.1
Sequence conflict1286 – 12905THGDQ → DARRS in AAA23904. Ref.1
Sequence conflict13731G → A in AAA23904. Ref.1
Sequence conflict13761G → R in AAA23904. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P09831-1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 7524A143B5DD4F9A

FASTA1,517166,710
        10         20         30         40         50         60 
MTRKPRRHAL SVPVRSGSEV GFPQSLGEVH DMLYDKSLER DNCGFGLIAH IEGEPSHKVV 

        70         80         90        100        110        120 
RTAIHALARM QHRGAILADG KTGDGCGLLL QKPDRFFRIV AQERGWRLAK NYAVGMLFLN 

       130        140        150        160        170        180 
KDPELAAAAR RIVEEELQRE TLSIVGWRDV PTNEGVLGEI ALSSLPRIEQ IFVNAPAGWR 

       190        200        210        220        230        240 
PRDMERRLFI ARRRIEKRLE ADKDFYVCSL SNLVNIYKGL CMPTDLPRFY LDLADLRLES 

       250        260        270        280        290        300 
AICLFHQRFS TNTVPRWPLA QPFRYLAHNG EINTITGNRQ WARARTYKFQ TPLIPDLHDA 

       310        320        330        340        350        360 
APFVNETGSD SSSMDNMLEL LLAGGMDIIR AMRLLVPPAW QNNPDMDPEL RAFFDFNSMH 

       370        380        390        400        410        420 
MEPWDGPAGI VMSDGRFAAC NLDRNGLRPA RYVITKDKLI TCASEVGIWD YQPDEVVEKG 

       430        440        450        460        470        480 
RVGPGELMVI DTRSGRILHS AETDDDLKSR HPYKEWMEKN VRRLVPFEDL PDEEVGSREL 

       490        500        510        520        530        540 
DDDTLASYQK QFNYSAEELD SVIRVLGENG QEAVGSMGDD TPFAVLSSQP RIIYDYFRQQ 

       550        560        570        580        590        600 
FAQVTNPPID PLREAHVMSL ATSIGREMNV FCEAEGQAHR LSFKSPILLY SDFKQLTTMK 

       610        620        630        640        650        660 
EEHYRADTLD ITFDVTKTTL EATVKELCDK AEKMVRSGTV LLVLSDRNIA KDRLPVPAPM 

       670        680        690        700        710        720 
AVGAIQTRLV DQSLRCDANI IVETASARDP HHFAVLLGFG ATAIYPYLAY ETLGRLVDTH 

       730        740        750        760        770        780 
AIAKDYRTVM LNYRNGINKG LYKIMSKMGI STIASYRCSK LFEAVGLHDD VVGLCFQGAV 

       790        800        810        820        830        840 
SRIGGASFED FQQDLLNLSK RAWLARKPIS QGGLLKYVHG GEYHAYNPDV VRTLQQAVQS 

       850        860        870        880        890        900 
GEYSDYQEYA KLVNERPATT LRDLLAITPG ENAVNIADVE PASELFKRFD TAAMSIGALS 

       910        920        930        940        950        960 
PEAHEALAEA MNSIGGNSNS GEGGEDPARY GTNKVSRIKQ VASGRFGVTP AYLVNADVIQ 

       970        980        990       1000       1010       1020 
IKVAQGAKPG EGGQLPGDKV TPYIAKLRYS VPGVTLISPP PHHDIYSIED LAQLIFDLKQ 

      1030       1040       1050       1060       1070       1080 
VNPKAMISVK LVSEPGVGTI ATGVAKAYAD LITIAGYDGG TGASPLSSVK YAGCPWELGL 

      1090       1100       1110       1120       1130       1140 
VETQQALVAN GLRHKIRLQV DGGLKTGVDI IKAAILGAES FGFGTGPMVA LGCKYLRICH 

      1150       1160       1170       1180       1190       1200 
LNNCATGVAT QDDKLRKNHY HGLPFKVTNY FEFIARETRE LMAQLGVTRL VDLIGRTDLL 

      1210       1220       1230       1240       1250       1260 
KELDGFTAKQ QKLALSKLLE TAEPHPGKAL YCTENNPPFD NGLLNAQLLQ QAKPFVDERQ 

      1270       1280       1290       1300       1310       1320 
SKTFWFDIRN TDRSVGASLS GYIAQTHGDQ GLAADPIKAY FNGTAGQSFG VWNAGGVELY 

      1330       1340       1350       1360       1370       1380 
LTGDANDYVG KGMAGGLIAI RPPVGSAFRS HEASIIGNTC LYGATGGRLY AAGRAGERFG 

      1390       1400       1410       1420       1430       1440 
VRNSGAITVV EGIGDNGCEY MTGGIVCILG KTGVNFGAGM TGGFAYVLDE SGDFRKRVNP 

      1450       1460       1470       1480       1490       1500 
ELVEVLSVDA LAIHEEHLRG LITEHVQHTG SQRGEEILAN WSTFATKFAL VKPKSSDVKA 

      1510 
LLGHRSRSAA ELRVQAQ 

« Hide

References

« Hide 'large scale' references
[1]"Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12."
Oliver G., Gosset G., Sanchez-Pescador R., Lozoya E., Ku L.M., Flores N., Becerril B., Valle F., Bolivar F.
Gene 60:1-11(1987) [PubMed: 3326786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Mutations affecting the Shine-Dalgarno sequences of the untranslated region of the Escherichia coli gltBDF operon."
Velazquez L., Camarena L., Reyes J.L., Bastarrachea F.
J. Bacteriol. 173:3261-3264(1991) [PubMed: 1673677] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-304.
[5]"Amino acid sequence analysis of the glutamate synthase enzyme from Escherichia coli K-12."
Gosset G., Merino E., Recillas F., Oliver G., Becerril B., Bolivar F.
Protein Seq. Data Anal. 2:9-16(1989) [PubMed: 2643092] [Abstract]
Cited for: DISCUSSION OF SEQUENCE.

Cross-references

Sequence databases

M18747 Genomic DNA. Translation: AAA23904.1.
U18997 Genomic DNA. Translation: AAA58014.1.
U00096 Genomic DNA. Translation: AAC76244.1.
AP009048 Genomic DNA. Translation: BAE77256.1.
M68876 Genomic DNA. Translation: AAA23906.1.
PIRF65112.
RefSeqAP_003755.1.
NP_417679.1.

3D structure databases

HSSPHSSP built from PDB template 1LM1 based on UniProtKB P55038.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9802N.
IntActP09831. 8 interactions.

Genome annotation databases

GeneID947724.
GenomeReviewsGene locus JW3179 in contig AP009048_GR.
Gene locus b3212 in contig U00096_GR.
KEGGecj:JW3179.
eco:b3212.

Organism-specific databases

EchoBASEEB0398.
EcoGeneEG10403. gltB.
CMRSearch...

Phylogenomic databases

HOGENOMP09831.
OMAP09831. DSAAMSI.

Enzyme and pathway databases

BioCycEcoCyc:GLUSYNLARGE-MON.
MetaCyc:GLUSYNLARGE-MON.
BRENDA1.4.1.13. 246.

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_ECOLI
AccessionPrimary (citable) accession number: P09831
Secondary accession number(s): Q2M900
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents