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P09831 (GLTB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length1486 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 (NADP(+) 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.

Sequence caution

The sequence AAA23904.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAA23906.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAA58014.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAE77256.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

gltDP098322EBI-551179,EBI-544293

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1111
PRO_0000011620
Chain12 – 14861475Glutamate synthase [NADPH] large chain
PRO_0000011621

Regions

Domain12 – 402391Glutamine amidotransferase type-2
Nucleotide binding1049 – 110153FMN By similarity

Sites

Active site121For GATase activity By similarity
Metal binding11021Iron-sulfur (3Fe-4S) By similarity
Metal binding11081Iron-sulfur (3Fe-4S) By similarity
Metal binding11131Iron-sulfur (3Fe-4S) By similarity

Experimental info

Sequence conflict74 – 785GWRLA → LAFR in AAA23904. Ref.1
Sequence conflict1091E → N in AAA23904. Ref.1
Sequence conflict189 – 20921LCMPT…LRLES → CVCRRICRVLSGSCGPASGM in AAA23904. Ref.1
Sequence conflict228 – 25124LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG in AAA23904. Ref.1
Sequence conflict228 – 25124LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG in AAA23906. Ref.4
Sequence conflict4291N → K in AAA23904. Ref.1
Sequence conflict5431A → T in AAA23904. Ref.1
Sequence conflict8321D → H in AAA23904. Ref.1
Sequence conflict1255 – 12595THGDQ → DARRS in AAA23904. Ref.1
Sequence conflict13421G → A in AAA23904. Ref.1
Sequence conflict13451G → R in AAA23904. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P09831 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 19C1E5B04F94A33D

FASTA1,486163,297
        10         20         30         40         50         60 
MLYDKSLERD NCGFGLIAHI EGEPSHKVVR TAIHALARMQ HRGAILADGK TGDGCGLLLQ 

        70         80         90        100        110        120 
KPDRFFRIVA QERGWRLAKN YAVGMLFLNK DPELAAAARR IVEEELQRET LSIVGWRDVP 

       130        140        150        160        170        180 
TNEGVLGEIA LSSLPRIEQI FVNAPAGWRP RDMERRLFIA RRRIEKRLEA DKDFYVCSLS 

       190        200        210        220        230        240 
NLVNIYKGLC MPTDLPRFYL DLADLRLESA ICLFHQRFST NTVPRWPLAQ PFRYLAHNGE 

       250        260        270        280        290        300 
INTITGNRQW ARARTYKFQT PLIPDLHDAA PFVNETGSDS SSMDNMLELL LAGGMDIIRA 

       310        320        330        340        350        360 
MRLLVPPAWQ NNPDMDPELR AFFDFNSMHM EPWDGPAGIV MSDGRFAACN LDRNGLRPAR 

       370        380        390        400        410        420 
YVITKDKLIT CASEVGIWDY QPDEVVEKGR VGPGELMVID TRSGRILHSA ETDDDLKSRH 

       430        440        450        460        470        480 
PYKEWMEKNV RRLVPFEDLP DEEVGSRELD DDTLASYQKQ FNYSAEELDS VIRVLGENGQ 

       490        500        510        520        530        540 
EAVGSMGDDT PFAVLSSQPR IIYDYFRQQF AQVTNPPIDP LREAHVMSLA TSIGREMNVF 

       550        560        570        580        590        600 
CEAEGQAHRL SFKSPILLYS DFKQLTTMKE EHYRADTLDI TFDVTKTTLE ATVKELCDKA 

       610        620        630        640        650        660 
EKMVRSGTVL LVLSDRNIAK DRLPVPAPMA VGAIQTRLVD QSLRCDANII VETASARDPH 

       670        680        690        700        710        720 
HFAVLLGFGA TAIYPYLAYE TLGRLVDTHA IAKDYRTVML NYRNGINKGL YKIMSKMGIS 

       730        740        750        760        770        780 
TIASYRCSKL FEAVGLHDDV VGLCFQGAVS RIGGASFEDF QQDLLNLSKR AWLARKPISQ 

       790        800        810        820        830        840 
GGLLKYVHGG EYHAYNPDVV RTLQQAVQSG EYSDYQEYAK LVNERPATTL RDLLAITPGE 

       850        860        870        880        890        900 
NAVNIADVEP ASELFKRFDT AAMSIGALSP EAHEALAEAM NSIGGNSNSG EGGEDPARYG 

       910        920        930        940        950        960 
TNKVSRIKQV ASGRFGVTPA YLVNADVIQI KVAQGAKPGE GGQLPGDKVT PYIAKLRYSV 

       970        980        990       1000       1010       1020 
PGVTLISPPP HHDIYSIEDL AQLIFDLKQV NPKAMISVKL VSEPGVGTIA TGVAKAYADL 

      1030       1040       1050       1060       1070       1080 
ITIAGYDGGT GASPLSSVKY AGCPWELGLV ETQQALVANG LRHKIRLQVD GGLKTGVDII 

      1090       1100       1110       1120       1130       1140 
KAAILGAESF GFGTGPMVAL GCKYLRICHL NNCATGVATQ DDKLRKNHYH GLPFKVTNYF 

      1150       1160       1170       1180       1190       1200 
EFIARETREL MAQLGVTRLV DLIGRTDLLK ELDGFTAKQQ KLALSKLLET AEPHPGKALY 

      1210       1220       1230       1240       1250       1260 
CTENNPPFDN GLLNAQLLQQ AKPFVDERQS KTFWFDIRNT DRSVGASLSG YIAQTHGDQG 

      1270       1280       1290       1300       1310       1320 
LAADPIKAYF NGTAGQSFGV WNAGGVELYL TGDANDYVGK GMAGGLIAIR PPVGSAFRSH 

      1330       1340       1350       1360       1370       1380 
EASIIGNTCL YGATGGRLYA AGRAGERFGV RNSGAITVVE GIGDNGCEYM TGGIVCILGK 

      1390       1400       1410       1420       1430       1440 
TGVNFGAGMT GGFAYVLDES GDFRKRVNPE LVEVLSVDAL AIHEEHLRGL ITEHVQHTGS 

      1450       1460       1470       1480 
QRGEEILANW STFATKFALV KPKSSDVKAL LGHRSRSAAE LRVQAQ

« 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273.
[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] [Europe PMC] [Abstract]
Cited for: DISCUSSION OF SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M18747 Genomic DNA. Translation: AAA23904.1. Different initiation.
U18997 Genomic DNA. Translation: AAA58014.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76244.2.
AP009048 Genomic DNA. Translation: BAE77256.1. Different initiation.
M68876 Genomic DNA. Translation: AAA23906.1. Different initiation.
PIRF65112.
RefSeqNP_417679.2. NC_000913.2.
YP_491397.1. NC_007779.1.

3D structure databases

ProteinModelPortalP09831.
SMRP09831. Positions 1266-1416.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9802N.
IntActP09831. 8 interactions.
MINTMINT-1248755.
STRING511145.b3212.

Protein family/group databases

MEROPSC44.003.

Proteomic databases

PaxDbP09831.
PRIDEP09831.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76244; AAC76244; b3212.
BAE77256; BAE77256; BAE77256.
GeneID12934216.
947724.
KEGGecj:Y75_p3132.
eco:b3212.
PATRIC32121846. VBIEscCol129921_3307.

Organism-specific databases

EchoBASEEB0398.
EcoGeneEG10403. gltB.

Phylogenomic databases

eggNOGCOG0069.
HOGENOMHOG000031558.
KOK00265.
ProtClustDBPRK11750.

Enzyme and pathway databases

BioCycEcoCyc:GLUSYNLARGE-MONOMER.
ECOL316407:JW3179-MONOMER.
MetaCyc:GLUSYNLARGE-MONOMER.
BRENDA1.4.1.13. 2026.
UniPathwayUPA00045.
UPA00634; UER00689.

Gene expression databases

GenevestigatorP09831.

Family and domain databases

Gene3D2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
InterProIPR013785. Aldolase_TIM.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR002489. Glu_synth_asu_C.
IPR002932. Glu_synth_centr_C.
IPR006982. Glu_synth_centr_N.
[Graphical view]
PfamPF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
[Graphical view]
SUPFAMSSF69336. Glu_synthase_C. 1 hit.
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 30, 2010
Last modified: May 1, 2013
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents