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Protein

Glutamate synthase [NADPH] large chain

Gene

gltA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 (gltB), Glutamate synthase [NADPH] large chain (gltA)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei22 – 221For GATase activityBy similarity
Metal bindingi1113 – 11131Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1119 – 11191Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1124 – 11241Iron-sulfur (3Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1060 – 111253FMNBy similarityAdd
BLAST

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

BioCyciBSUB:BSU18450-MONOMER.
RETL1328306-WGS:GSTH-3634-MONOMER.
BRENDAi1.4.1.13. 658.
SABIO-RKP39812.
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):
NADPH-GOGAT
Gene namesi
Name:gltA
Ordered Locus Names:BSU18450
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15201520Glutamate synthase [NADPH] large chainPRO_0000170797Add
BLAST

Proteomic databases

PaxDbiP39812.

Expressioni

Inductioni

The gltAB operon is positively regulated by GltC and negatively regulated by TnrA under nitrogen-limited conditions.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP39812. 1 interaction.
MINTiMINT-8364926.
STRINGi224308.Bsubs1_010100010166.

Structurei

3D structure databases

ProteinModelPortaliP39812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 415394Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiP39812.
KOiK00265.
OMAiEHMWTPD.
OrthoDBiEOG60W7PX.
PhylomeDBiP39812.

Family and domain databases

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.

P39812-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTYNQMPKAQ GLYRPEFEHD ACGIGLYAHL KGKQTHDIVK QGLKMLCQLD
60 70 80 90 100
HRGGQGSDPD TGDGAGLLVQ IPDAFFRKEC KNINLPEKER YGVGMVFFSQ
110 120 130 140 150
KEDERKKIEK QINALIEQEG QVVLGWRTVP VNVGKIGTVA QKSCPFVRQV
160 170 180 190 200
FIGASSDLKD NLSFERKLYV IRKQAENWGV TEGLDFYFAS LSSQTIVYKG
210 220 230 240 250
LLTPEQVDAF YSDLQDEAFV SAFALVHSRF STNTFPTWER AHPNRYLVHN
260 270 280 290 300
GEINTLRGNI NWMRAREQQF VSESFGEDLN KILPILNADG SDSSILDNAF
310 320 330 340 350
EFFVMAGRKP AHTAMMLIPE PWTENTHMSK EKRAFYEYHS SLMEPWDGPT
360 370 380 390 400
AISFTDGKQI GAILDRNGLR PARYYVTKDD YIIFSSEVGV IEVEQENVLY
410 420 430 440 450
KNRLEPGKML LIDLEEGRII SDEEVKTQIA TEYPYQKWLE EELVQVNPDP
460 470 480 490 500
ESREEEQFSD LLTRQKAFGY TYEDIQKYLI PVIKEGKDPL GSMGNDAPLA
510 520 530 540 550
VLSDRAQSLF NYFKQLFAQV TNPPIDAIRE QLVTSTMTWL GAEGDLLHPS
560 570 580 590 600
ERNVRRIKLY TPVLSNEQFY ALKTIVHPDL KSQKIDVLFS EDLERGLKDM
610 620 630 640 650
FTQAEKAISQ GVSLLILSDK KMNERLTPIP PLLAVSALHQ HLIRKGLRTK
660 670 680 690 700
VSIIVESGEA REVHHFAALI GYGADAINPY LAYATYKQEI DEGRLDISYE
710 720 730 740 750
EAVSKYGKSI TEGVVKVMSK MGISTVQSYR GAQIFEAVGI SRDVIDRYFS
760 770 780 790 800
GTASQLGGID LQTIAEEAQR RHREAYQDDY SKTLEPGSDF QWRNGGEHHA
810 820 830 840 850
FNPKTIHTLQ WACRRNDYNL FKQYTKAADE ERIGFLRNLF AFDGNRKPLK
860 870 880 890 900
LEEVESAESI VKRFKTGAMS FGSLSKEAHE ALAIAMNRLG GKSNSGEGGE
910 920 930 940 950
DPKRFVPDEN GDDRRSAIKQ IASGRFGVKS HYLVNADELQ IKMAQGAKPG
960 970 980 990 1000
EGGQLPGNKV YPWVADVRGS TPGVGLISPP PHHDIYSIED LAQLIHDLKN
1010 1020 1030 1040 1050
ANRDARISVK LVSKAGVGTI AAGVAKATAD VIVISGYDGG TGASPKTSIK
1060 1070 1080 1090 1100
HTGLPWELGL AEAHQTLMLN GLRDRVVLET DGKLMTGRDV VMAALLGAEE
1110 1120 1130 1140 1150
FGFATAPLVV LGCVMMRACH LDTCPVGVAT QNPELRKKFM GDPDHIVNYM
1160 1170 1180 1190 1200
LFIAEEVREY MAALGFKTFD EMIGRTDVLH ASERAKEHWK ASQLDLSTLL
1210 1220 1230 1240 1250
YQPEGVRTFQ SPQNHKIDQS LDITTILPAV QEAIESGKEA DISIEINNTN
1260 1270 1280 1290 1300
RVAGTITGSE ISKRYGEEGL PEDTIKLHFT GSAGQSFGAF VPKGMTLYLD
1310 1320 1330 1340 1350
GDSNDYVGKG LSGGKIIVKS SEGFNSASDD NVIIGNVAFY GATSGEAYIN
1360 1370 1380 1390 1400
GRAGERFAVR NSGVNVVVEG IGDHGCEYMT GGSVVVLGDV GKNFAAGMSG
1410 1420 1430 1440 1450
GIAYVLTEDV KAFKRKCNLE MILFESLEDE KEIQQIKAML ERHTAYTNSQ
1460 1470 1480 1490 1500
KAEDLLDQWE DSVKKFVKVI PKNYKQMLAS IEEQKAAGLS DEEAIMFAFE
1510 1520
ANTKPKQNTA ASGQKQAVVQ
Length:1,520
Mass (Da):168,772
Last modified:June 16, 2009 - v3
Checksum:i156A22E65A8CC423
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13728.2.
M28509 Unassigned DNA. Translation: AAA16438.1.
PIRiG69634.
RefSeqiNP_389727.2. NC_000964.3.
WP_009967365.1. NZ_CP010052.1.

Genome annotation databases

EnsemblBacteriaiCAB13728; CAB13728; BSU18450.
GeneIDi940024.
KEGGibsu:BSU18450.
PATRICi18975529. VBIBacSub10457_1955.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13728.2.
M28509 Unassigned DNA. Translation: AAA16438.1.
PIRiG69634.
RefSeqiNP_389727.2. NC_000964.3.
WP_009967365.1. NZ_CP010052.1.

3D structure databases

ProteinModelPortaliP39812.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP39812. 1 interaction.
MINTiMINT-8364926.
STRINGi224308.Bsubs1_010100010166.

Protein family/group databases

MEROPSiC44.003.

Proteomic databases

PaxDbiP39812.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13728; CAB13728; BSU18450.
GeneIDi940024.
KEGGibsu:BSU18450.
PATRICi18975529. VBIBacSub10457_1955.

Phylogenomic databases

eggNOGiENOG4105CBC. Bacteria.
COG0067. LUCA.
COG0069. LUCA.
COG0070. LUCA.
HOGENOMiHOG000031558.
InParanoidiP39812.
KOiK00265.
OMAiEHMWTPD.
OrthoDBiEOG60W7PX.
PhylomeDBiP39812.

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00689.
BioCyciBSUB:BSU18450-MONOMER.
RETL1328306-WGS:GSTH-3634-MONOMER.
BRENDAi1.4.1.13. 658.
SABIO-RKP39812.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 1412.
  3. "Positive regulation of glutamate biosynthesis in Bacillus subtilis."
    Bohannon D.E., Sonenshein A.L.
    J. Bacteriol. 171:4718-4727(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  4. "Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression."
    Belitsky B.R., Wray L.V. Jr., Fisher S.H., Bohannon D.E., Sonenshein A.L.
    J. Bacteriol. 182:5939-5947(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY TNRA.
  5. "Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box."
    Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.
    Mol. Microbiol. 49:157-165(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY TNRA.

Entry informationi

Entry nameiGLTA_BACSU
AccessioniPrimary (citable) accession number: P39812
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 16, 2009
Last modified: June 8, 2016
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.