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Protein

Glutamate synthase [NADPH] large chain

Gene

gltB

Organism
Azospirillum brasilense
Status
Reviewed-Annotation score: Annotation score: 4 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] large chain (gltB), Glutamate synthase [NADPH] small chain (gltD)
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 sitei37 – 371For GATase activityBy similarity
Metal bindingi1138 – 11381Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1144 – 11441Iron-sulfur (3Fe-4S)By similarity
Metal bindingi1149 – 11491Iron-sulfur (3Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1085 – 114258FMNBy similarityAdd
BLAST
Nucleotide bindingi1086 – 114257FMNBy 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

BioCyciMetaCyc:MONOMER-13079.
BRENDAi1.4.1.13. 611.
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
OrganismiAzospirillum brasilense
Taxonomic identifieri192 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 36361 PublicationPRO_0000011618Add
BLAST
Chaini37 – 15151479Glutamate synthase [NADPH] large chainPRO_0000011619Add
BLAST

Keywords - PTMi

Zymogen

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
1515
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 444Combined sources
Helixi51 – 6111Combined sources
Helixi65 – 673Combined sources
Beta strandi82 – 854Combined sources
Helixi88 – 9710Combined sources
Beta strandi107 – 1148Combined sources
Helixi119 – 13517Combined sources
Beta strandi139 – 1457Combined sources
Helixi150 – 1523Combined sources
Helixi155 – 1606Combined sources
Beta strandi163 – 1708Combined sources
Helixi177 – 19822Combined sources
Beta strandi204 – 21411Combined sources
Beta strandi217 – 2193Combined sources
Helixi221 – 2233Combined sources
Helixi224 – 2274Combined sources
Helixi229 – 2324Combined sources
Beta strandi238 – 2458Combined sources
Beta strandi262 – 2687Combined sources
Helixi273 – 28311Combined sources
Helixi284 – 2863Combined sources
Helixi293 – 2953Combined sources
Helixi296 – 2994Combined sources
Helixi309 – 32214Combined sources
Helixi327 – 3348Combined sources
Helixi347 – 35913Combined sources
Beta strandi365 – 3717Combined sources
Beta strandi373 – 3808Combined sources
Beta strandi390 – 3945Combined sources
Beta strandi397 – 4015Combined sources
Beta strandi403 – 4053Combined sources
Helixi412 – 4143Combined sources
Beta strandi415 – 4206Combined sources
Beta strandi426 – 4305Combined sources
Turni431 – 4344Combined sources
Beta strandi435 – 4373Combined sources
Helixi439 – 44810Combined sources
Turni449 – 4513Combined sources
Helixi452 – 4565Combined sources
Helixi464 – 4718Combined sources
Helixi481 – 4888Combined sources
Turni489 – 4913Combined sources
Helixi494 – 4985Combined sources
Turni499 – 5013Combined sources
Helixi502 – 5076Combined sources
Helixi522 – 5243Combined sources
Helixi531 – 5333Combined sources
Beta strandi535 – 5373Combined sources
Beta strandi542 – 5443Combined sources
Turni549 – 5524Combined sources
Helixi553 – 5553Combined sources
Beta strandi560 – 5634Combined sources
Helixi573 – 5753Combined sources
Beta strandi578 – 5825Combined sources
Helixi588 – 59811Combined sources
Helixi599 – 6013Combined sources
Beta strandi602 – 6065Combined sources
Beta strandi608 – 6114Combined sources
Helixi617 – 63519Combined sources
Beta strandi639 – 6435Combined sources
Beta strandi651 – 6533Combined sources
Helixi656 – 66813Combined sources
Turni669 – 6713Combined sources
Helixi673 – 6753Combined sources
Beta strandi677 – 6815Combined sources
Helixi688 – 6958Combined sources
Turni696 – 6983Combined sources
Beta strandi700 – 7034Combined sources
Helixi705 – 71511Combined sources
Turni716 – 7227Combined sources
Helixi725 – 74521Combined sources
Turni746 – 7483Combined sources
Helixi752 – 7554Combined sources
Beta strandi761 – 7666Combined sources
Helixi768 – 7747Combined sources
Beta strandi775 – 7773Combined sources
Helixi787 – 80216Combined sources
Beta strandi814 – 8163Combined sources
Beta strandi819 – 8224Combined sources
Helixi828 – 84013Combined sources
Helixi843 – 85412Combined sources
Helixi861 – 8644Combined sources
Beta strandi865 – 8673Combined sources
Helixi876 – 8783Combined sources
Helixi882 – 8865Combined sources
Beta strandi889 – 8935Combined sources
Helixi901 – 91313Combined sources
Beta strandi917 – 9193Combined sources
Helixi927 – 9293Combined sources
Beta strandi930 – 9323Combined sources
Beta strandi942 – 9465Combined sources
Helixi955 – 9584Combined sources
Beta strandi962 – 9676Combined sources
Turni974 – 9763Combined sources
Helixi982 – 9843Combined sources
Helixi987 – 9937Combined sources
Helixi1013 – 102614Combined sources
Beta strandi1031 – 10377Combined sources
Helixi1042 – 105110Combined sources
Beta strandi1055 – 10606Combined sources
Beta strandi1067 – 10704Combined sources
Helixi1073 – 10764Combined sources
Helixi1081 – 109313Combined sources
Turni1094 – 10963Combined sources
Beta strandi1100 – 11089Combined sources
Helixi1112 – 11209Combined sources
Beta strandi1124 – 11274Combined sources
Helixi1130 – 11367Combined sources
Turni1144 – 11474Combined sources
Beta strandi1152 – 11543Combined sources
Helixi1160 – 11623Combined sources
Helixi1168 – 118922Combined sources
Helixi1195 – 11973Combined sources
Helixi1201 – 12033Combined sources
Beta strandi1204 – 12063Combined sources
Helixi1220 – 12234Combined sources
Helixi1248 – 12547Combined sources
Helixi1256 – 12616Combined sources
Beta strandi1265 – 12717Combined sources
Helixi1280 – 128910Combined sources
Turni1290 – 12934Combined sources
Beta strandi1299 – 130810Combined sources
Turni1312 – 13154Combined sources
Beta strandi1320 – 13289Combined sources
Turni1332 – 13354Combined sources
Beta strandi1337 – 13448Combined sources
Helixi1353 – 13553Combined sources
Beta strandi1356 – 13594Combined sources
Turni1363 – 13664Combined sources
Beta strandi1369 – 137810Combined sources
Turni1380 – 13856Combined sources
Beta strandi1387 – 13948Combined sources
Turni1400 – 14034Combined sources
Beta strandi1406 – 14094Combined sources
Beta strandi1417 – 14193Combined sources
Turni1420 – 14223Combined sources
Beta strandi1425 – 14284Combined sources
Helixi1437 – 14404Combined sources
Helixi1443 – 14453Combined sources
Beta strandi1446 – 14494Combined sources
Helixi1456 – 147116Combined sources
Helixi1474 – 14818Combined sources
Helixi1483 – 14875Combined sources
Beta strandi1492 – 14954Combined sources
Helixi1496 – 15016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EA0X-ray3.00A/B37-1515[»]
2VDCelectron microscopy9.50A/B/C/D/E/F37-1508[»]
ProteinModelPortaliQ05755.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05755.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 432396Glutamine 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

KOiK00265.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05755-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTELNQGEQ FVADFRANAA ALTTANAYNP EDEHDACGVG FIAAIDGKPR
60 70 80 90 100
RSVVEKGIEA LKAVWHRGAV DADGKTGDGA GIHVAVPQKF FKDHVKVIGH
110 120 130 140 150
RAPDNKLAVG QVFLPRISLD AQEACRCIVE TEILAFGYYI YGWRQVPINV
160 170 180 190 200
DIIGEKANAT RPEIEQIIVG NNKGVSDEQF ELDLYIIRRR IEKAVKGEQI
210 220 230 240 250
NDFYICSLSA RSIIYKGMFL AEQLTTFYPD LLDERFESDF AIYHQRYSTN
260 270 280 290 300
TFPTWPLAQP FRMLAHNGEI NTVKGNVNWM KAHETRMEHP AFGTHMQDLK
310 320 330 340 350
PVIGVGLSDS GSLDTVFEVM VRAGRTAPMV KMMLVPQALT SSQTTPDNHK
360 370 380 390 400
ALIQYCNSVM EPWDGPAALA MTDGRWVVGG MDRNGLRPMR YTITTDGLII
410 420 430 440 450
GGSETGMVKI DETQVIEKGR LGPGEMIAVD LQSGKLYRDR ELKDHLATLK
460 470 480 490 500
PWDKWVQNTT HLDELVKTAS LKGEPSDMDK AELRRRQQAF GLTMEDMELI
510 520 530 540 550
LHPMVEDGKE AIGSMGDDSP IAVLSDKYRG LHHFFRQNFS QVTNPPIDSL
560 570 580 590 600
RERRVMSLKT RLGNLGNILD EDETQTRLLQ LESPVLTTAE FRAMRDYMGD
610 620 630 640 650
TAAEIDATFP VDGGPEALRD ALRRIRQETE DAVRGGATHV ILTDEAMGPA
660 670 680 690 700
RAAIPAILAT GAVHTHLIRS NLRTFTSLNV RTAEGLDTHY FAVLIGVGAT
710 720 730 740 750
TVNAYLAQEA IAERHRRGLF GSMPLEKGMA NYKKAIDDGL LKIMSKMGIS
760 770 780 790 800
VISSYRGGGN FEAIGLSRAL VAEHFPAMVS RISGIGLNGI QKKVLEQHAT
810 820 830 840 850
AYNEEVVALP VGGFYRFRKS GDRHGWEGGV IHTLQQAVTN DSYTTFKKYS
860 870 880 890 900
EQVNKRPPMQ LRDLLELRST KAPVPVDEVE SITAIRKRFI TPGMSMGALS
910 920 930 940 950
PEAHGTLNVA MNRIGAKSDS GEGGEDPARF RPDKNGDNWN SAIKQVASGR
960 970 980 990 1000
FGVTAEYLNQ CRELEIKVAQ GAKPGEGGQL PGFKVTEMIA RLRHSTPGVM
1010 1020 1030 1040 1050
LISPPPHHDI YSIEDLAQLI YDLKQINPDA KVTVKLVSRS GIGTIAAGVA
1060 1070 1080 1090 1100
KANADIILIS GNSGGTGASP QTSIKFAGLP WEMGLSEVHQ VLTLNRLRHR
1110 1120 1130 1140 1150
VRLRTDGGLK TGRDIVIAAM LGAEEFGIGT ASLIAMGCIM VRQCHSNTCP
1160 1170 1180 1190 1200
VGVCVQDDKL RQKFVGTPEK VVNLFTFLAE EVREILAGLG FRSLNEVIGR
1210 1220 1230 1240 1250
TDLLHQVSRG AEHLDDLDLN PRLAQVDPGE NARYCTLQGR NEVPDTLDAR
1260 1270 1280 1290 1300
IVADARPLFE EGEKMQLAYN ARNTQRAIGT RLSSMVTRKF GMFGLQPGHI
1310 1320 1330 1340 1350
TIRLRGTAGQ SLGAFAVQGI KLEVMGDAND YVGKGLSGGT IVVRPTTSSP
1360 1370 1380 1390 1400
LETNKNTIIG NTVLYGATAG KLFAAGQAGE RFAVRNSGAT VVVEGCGSNG
1410 1420 1430 1440 1450
CEYMTGGTAV ILGRVGDNFA AGMTGGMAYV YDLDDSLPLY INDESVIFQR
1460 1470 1480 1490 1500
IEVGHYESQL KHLIEEHVTE TQSRFAAEIL NDWAREVTKF WQVVPKEMLN
1510
RLEVPVHLPK AISAE
Length:1,515
Mass (Da):166,018
Last modified:February 1, 1995 - v1
Checksum:iED913218DBFCEE92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192408 Genomic DNA. Translation: AAA22179.1.
X71632 Genomic DNA. Translation: CAA50639.1.
PIRiB46602.

Genome annotation databases

KEGGiag:AAA22179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192408 Genomic DNA. Translation: AAA22179.1.
X71632 Genomic DNA. Translation: CAA50639.1.
PIRiB46602.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EA0X-ray3.00A/B37-1515[»]
2VDCelectron microscopy9.50A/B/C/D/E/F37-1508[»]
ProteinModelPortaliQ05755.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC44.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA22179.

Phylogenomic databases

KOiK00265.

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00689.
BioCyciMetaCyc:MONOMER-13079.
BRENDAi1.4.1.13. 611.

Miscellaneous databases

EvolutionaryTraceiQ05755.

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...

Entry informationi

Entry nameiGLTB_AZOBR
AccessioniPrimary (citable) accession number: Q05755
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 98 of the entry and version 1 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

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.