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Protein

Glutamate synthase [NADPH] large chain

Gene

gltB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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 (NADP(+) route).
Proteins known to be involved in this subpathway in this organism are:
  1. Glutamate synthase [NADPH] small chain (gltD), Glutamate synthase [NADPH] large chain (gltB)
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 (NADP(+) 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)DescriptionActionsGraphical viewLength
Active sitei12For GATase activityBy similarity1
Metal bindingi1102Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1108Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1113Iron-sulfur (3Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1049 – 1101FMNBy similarityAdd BLAST53

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, NADP

Enzyme and pathway databases

BioCyciEcoCyc:GLUSYNLARGE-MONOMER.
ECOL316407:JW3179-MONOMER.
MetaCyc:GLUSYNLARGE-MONOMER.
BRENDAi1.4.1.13. 2026.
UniPathwayiUPA00045.
UPA00634; UER00689.

Protein family/group databases

MEROPSiC44.003.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:gltB
Synonyms:aspB
Ordered Locus Names:b3212, JW3179
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10403. gltB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000116201 – 11Add BLAST11
ChainiPRO_000001162112 – 1486Glutamate synthase [NADPH] large chainAdd BLAST1475

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiP09831.
PRIDEiP09831.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
gltDP098322EBI-551179,EBI-544293

Protein-protein interaction databases

BioGridi4263210. 332 interactors.
DIPiDIP-9802N.
IntActiP09831. 8 interactors.
MINTiMINT-1248755.
STRINGi511145.b3212.

Structurei

3D structure databases

ProteinModelPortaliP09831.
SMRiP09831.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 402Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST391

Sequence similaritiesi

Belongs to the glutamate synthase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105CBC. Bacteria.
COG0067. LUCA.
COG0069. LUCA.
COG0070. LUCA.
HOGENOMiHOG000031558.
InParanoidiP09831.
KOiK00265.
PhylomeDBiP09831.

Family and domain databases

CDDicd02808. GltS_FMN. 1 hit.
Gene3Di2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.60.20.10. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017932. GATase_2_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR002932. Glu_synthdom.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 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.

P09831-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYDKSLERD NCGFGLIAHI EGEPSHKVVR TAIHALARMQ HRGAILADGK
60 70 80 90 100
TGDGCGLLLQ KPDRFFRIVA QERGWRLAKN YAVGMLFLNK DPELAAAARR
110 120 130 140 150
IVEEELQRET LSIVGWRDVP TNEGVLGEIA LSSLPRIEQI FVNAPAGWRP
160 170 180 190 200
RDMERRLFIA RRRIEKRLEA DKDFYVCSLS NLVNIYKGLC MPTDLPRFYL
210 220 230 240 250
DLADLRLESA ICLFHQRFST NTVPRWPLAQ PFRYLAHNGE INTITGNRQW
260 270 280 290 300
ARARTYKFQT PLIPDLHDAA PFVNETGSDS SSMDNMLELL LAGGMDIIRA
310 320 330 340 350
MRLLVPPAWQ NNPDMDPELR AFFDFNSMHM EPWDGPAGIV MSDGRFAACN
360 370 380 390 400
LDRNGLRPAR YVITKDKLIT CASEVGIWDY QPDEVVEKGR VGPGELMVID
410 420 430 440 450
TRSGRILHSA ETDDDLKSRH PYKEWMEKNV RRLVPFEDLP DEEVGSRELD
460 470 480 490 500
DDTLASYQKQ FNYSAEELDS VIRVLGENGQ EAVGSMGDDT PFAVLSSQPR
510 520 530 540 550
IIYDYFRQQF AQVTNPPIDP LREAHVMSLA TSIGREMNVF CEAEGQAHRL
560 570 580 590 600
SFKSPILLYS DFKQLTTMKE EHYRADTLDI TFDVTKTTLE ATVKELCDKA
610 620 630 640 650
EKMVRSGTVL LVLSDRNIAK DRLPVPAPMA VGAIQTRLVD QSLRCDANII
660 670 680 690 700
VETASARDPH HFAVLLGFGA TAIYPYLAYE TLGRLVDTHA IAKDYRTVML
710 720 730 740 750
NYRNGINKGL YKIMSKMGIS TIASYRCSKL FEAVGLHDDV VGLCFQGAVS
760 770 780 790 800
RIGGASFEDF QQDLLNLSKR AWLARKPISQ GGLLKYVHGG EYHAYNPDVV
810 820 830 840 850
RTLQQAVQSG EYSDYQEYAK LVNERPATTL RDLLAITPGE NAVNIADVEP
860 870 880 890 900
ASELFKRFDT AAMSIGALSP EAHEALAEAM NSIGGNSNSG EGGEDPARYG
910 920 930 940 950
TNKVSRIKQV ASGRFGVTPA YLVNADVIQI KVAQGAKPGE GGQLPGDKVT
960 970 980 990 1000
PYIAKLRYSV PGVTLISPPP HHDIYSIEDL AQLIFDLKQV NPKAMISVKL
1010 1020 1030 1040 1050
VSEPGVGTIA TGVAKAYADL ITIAGYDGGT GASPLSSVKY AGCPWELGLV
1060 1070 1080 1090 1100
ETQQALVANG LRHKIRLQVD GGLKTGVDII KAAILGAESF GFGTGPMVAL
1110 1120 1130 1140 1150
GCKYLRICHL NNCATGVATQ DDKLRKNHYH GLPFKVTNYF EFIARETREL
1160 1170 1180 1190 1200
MAQLGVTRLV DLIGRTDLLK ELDGFTAKQQ KLALSKLLET AEPHPGKALY
1210 1220 1230 1240 1250
CTENNPPFDN GLLNAQLLQQ AKPFVDERQS KTFWFDIRNT DRSVGASLSG
1260 1270 1280 1290 1300
YIAQTHGDQG LAADPIKAYF NGTAGQSFGV WNAGGVELYL TGDANDYVGK
1310 1320 1330 1340 1350
GMAGGLIAIR PPVGSAFRSH EASIIGNTCL YGATGGRLYA AGRAGERFGV
1360 1370 1380 1390 1400
RNSGAITVVE GIGDNGCEYM TGGIVCILGK TGVNFGAGMT GGFAYVLDES
1410 1420 1430 1440 1450
GDFRKRVNPE LVEVLSVDAL AIHEEHLRGL ITEHVQHTGS QRGEEILANW
1460 1470 1480
STFATKFALV KPKSSDVKAL LGHRSRSAAE LRVQAQ
Length:1,486
Mass (Da):163,297
Last modified:November 30, 2010 - v3
Checksum:i19C1E5B04F94A33D
GO

Sequence cautioni

The sequence AAA23904 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAA23906 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAA58014 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE77256 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74 – 78GWRLA → LAFR in AAA23904 (PubMed:3326786).Curated5
Sequence conflicti109E → N in AAA23904 (PubMed:3326786).Curated1
Sequence conflicti189 – 209LCMPT…LRLES → CVCRRICRVLSGSCGPASGM in AAA23904 (PubMed:3326786).CuratedAdd BLAST21
Sequence conflicti228 – 251LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG in AAA23904 (PubMed:3326786).CuratedAdd BLAST24
Sequence conflicti228 – 251LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG in AAA23906 (PubMed:1673677).CuratedAdd BLAST24
Sequence conflicti429N → K in AAA23904 (PubMed:3326786).Curated1
Sequence conflicti543A → T in AAA23904 (PubMed:3326786).Curated1
Sequence conflicti832D → H in AAA23904 (PubMed:3326786).Curated1
Sequence conflicti1255 – 1259THGDQ → DARRS in AAA23904 (PubMed:3326786).Curated5
Sequence conflicti1342G → A in AAA23904 (PubMed:3326786).Curated1
Sequence conflicti1345G → R in AAA23904 (PubMed:3326786).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF65112.
RefSeqiNP_417679.2. NC_000913.3.
WP_001300352.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76244; AAC76244; b3212.
BAE77256; BAE77256; BAE77256.
GeneIDi947724.
KEGGiecj:JW3179.
eco:b3212.
PATRICi32121846. VBIEscCol129921_3307.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF65112.
RefSeqiNP_417679.2. NC_000913.3.
WP_001300352.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP09831.
SMRiP09831.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263210. 332 interactors.
DIPiDIP-9802N.
IntActiP09831. 8 interactors.
MINTiMINT-1248755.
STRINGi511145.b3212.

Protein family/group databases

MEROPSiC44.003.

Proteomic databases

PaxDbiP09831.
PRIDEiP09831.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76244; AAC76244; b3212.
BAE77256; BAE77256; BAE77256.
GeneIDi947724.
KEGGiecj:JW3179.
eco:b3212.
PATRICi32121846. VBIEscCol129921_3307.

Organism-specific databases

EchoBASEiEB0398.
EcoGeneiEG10403. gltB.

Phylogenomic databases

eggNOGiENOG4105CBC. Bacteria.
COG0067. LUCA.
COG0069. LUCA.
COG0070. LUCA.
HOGENOMiHOG000031558.
InParanoidiP09831.
KOiK00265.
PhylomeDBiP09831.

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00689.
BioCyciEcoCyc:GLUSYNLARGE-MONOMER.
ECOL316407:JW3179-MONOMER.
MetaCyc:GLUSYNLARGE-MONOMER.
BRENDAi1.4.1.13. 2026.

Miscellaneous databases

PROiP09831.

Family and domain databases

CDDicd02808. GltS_FMN. 1 hit.
Gene3Di2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.60.20.10. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017932. GATase_2_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR002932. Glu_synthdom.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamiPF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLTB_ECOLI
AccessioniPrimary (citable) accession number: P09831
Secondary accession number(s): Q2M900
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 30, 2010
Last modified: November 2, 2016
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.