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Protein

Glutamate synthase [NADPH] large chain

Gene

gltB

Organism
Azospirillum brasilense
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] 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)DescriptionActionsGraphical viewLength
Active sitei37For GATase activityBy similarity1
Metal bindingi1138Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1144Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1149Iron-sulfur (3Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1085 – 1142FMNBy similarityAdd BLAST58
Nucleotide bindingi1086 – 1142FMNBy similarityAdd BLAST57

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)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000116181 – 361 PublicationAdd BLAST36
ChainiPRO_000001161937 – 1515Glutamate synthase [NADPH] large chainAdd BLAST1479

Keywords - PTMi

Zymogen

Interactioni

Subunit structurei

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

Structurei

Secondary structure

11515
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 44Combined sources4
Helixi51 – 61Combined sources11
Helixi65 – 67Combined sources3
Beta strandi82 – 85Combined sources4
Helixi88 – 97Combined sources10
Beta strandi107 – 114Combined sources8
Helixi119 – 135Combined sources17
Beta strandi139 – 145Combined sources7
Helixi150 – 152Combined sources3
Helixi155 – 160Combined sources6
Beta strandi163 – 170Combined sources8
Helixi177 – 198Combined sources22
Beta strandi204 – 214Combined sources11
Beta strandi217 – 219Combined sources3
Helixi221 – 223Combined sources3
Helixi224 – 227Combined sources4
Helixi229 – 232Combined sources4
Beta strandi238 – 245Combined sources8
Beta strandi262 – 268Combined sources7
Helixi273 – 283Combined sources11
Helixi284 – 286Combined sources3
Helixi293 – 295Combined sources3
Helixi296 – 299Combined sources4
Helixi309 – 322Combined sources14
Helixi327 – 334Combined sources8
Helixi347 – 359Combined sources13
Beta strandi365 – 371Combined sources7
Beta strandi373 – 380Combined sources8
Beta strandi390 – 394Combined sources5
Beta strandi397 – 401Combined sources5
Beta strandi403 – 405Combined sources3
Helixi412 – 414Combined sources3
Beta strandi415 – 420Combined sources6
Beta strandi426 – 430Combined sources5
Turni431 – 434Combined sources4
Beta strandi435 – 437Combined sources3
Helixi439 – 448Combined sources10
Turni449 – 451Combined sources3
Helixi452 – 456Combined sources5
Helixi464 – 471Combined sources8
Helixi481 – 488Combined sources8
Turni489 – 491Combined sources3
Helixi494 – 498Combined sources5
Turni499 – 501Combined sources3
Helixi502 – 507Combined sources6
Helixi522 – 524Combined sources3
Helixi531 – 533Combined sources3
Beta strandi535 – 537Combined sources3
Beta strandi542 – 544Combined sources3
Turni549 – 552Combined sources4
Helixi553 – 555Combined sources3
Beta strandi560 – 563Combined sources4
Helixi573 – 575Combined sources3
Beta strandi578 – 582Combined sources5
Helixi588 – 598Combined sources11
Helixi599 – 601Combined sources3
Beta strandi602 – 606Combined sources5
Beta strandi608 – 611Combined sources4
Helixi617 – 635Combined sources19
Beta strandi639 – 643Combined sources5
Beta strandi651 – 653Combined sources3
Helixi656 – 668Combined sources13
Turni669 – 671Combined sources3
Helixi673 – 675Combined sources3
Beta strandi677 – 681Combined sources5
Helixi688 – 695Combined sources8
Turni696 – 698Combined sources3
Beta strandi700 – 703Combined sources4
Helixi705 – 715Combined sources11
Turni716 – 722Combined sources7
Helixi725 – 745Combined sources21
Turni746 – 748Combined sources3
Helixi752 – 755Combined sources4
Beta strandi761 – 766Combined sources6
Helixi768 – 774Combined sources7
Beta strandi775 – 777Combined sources3
Helixi787 – 802Combined sources16
Beta strandi814 – 816Combined sources3
Beta strandi819 – 822Combined sources4
Helixi828 – 840Combined sources13
Helixi843 – 854Combined sources12
Helixi861 – 864Combined sources4
Beta strandi865 – 867Combined sources3
Helixi876 – 878Combined sources3
Helixi882 – 886Combined sources5
Beta strandi889 – 893Combined sources5
Helixi901 – 913Combined sources13
Beta strandi917 – 919Combined sources3
Helixi927 – 929Combined sources3
Beta strandi930 – 932Combined sources3
Beta strandi942 – 946Combined sources5
Helixi955 – 958Combined sources4
Beta strandi962 – 967Combined sources6
Turni974 – 976Combined sources3
Helixi982 – 984Combined sources3
Helixi987 – 993Combined sources7
Helixi1013 – 1026Combined sources14
Beta strandi1031 – 1037Combined sources7
Helixi1042 – 1051Combined sources10
Beta strandi1055 – 1060Combined sources6
Beta strandi1067 – 1070Combined sources4
Helixi1073 – 1076Combined sources4
Helixi1081 – 1093Combined sources13
Turni1094 – 1096Combined sources3
Beta strandi1100 – 1108Combined sources9
Helixi1112 – 1120Combined sources9
Beta strandi1124 – 1127Combined sources4
Helixi1130 – 1136Combined sources7
Turni1144 – 1147Combined sources4
Beta strandi1152 – 1154Combined sources3
Helixi1160 – 1162Combined sources3
Helixi1168 – 1189Combined sources22
Helixi1195 – 1197Combined sources3
Helixi1201 – 1203Combined sources3
Beta strandi1204 – 1206Combined sources3
Helixi1220 – 1223Combined sources4
Helixi1248 – 1254Combined sources7
Helixi1256 – 1261Combined sources6
Beta strandi1265 – 1271Combined sources7
Helixi1280 – 1289Combined sources10
Turni1290 – 1293Combined sources4
Beta strandi1299 – 1308Combined sources10
Turni1312 – 1315Combined sources4
Beta strandi1320 – 1328Combined sources9
Turni1332 – 1335Combined sources4
Beta strandi1337 – 1344Combined sources8
Helixi1353 – 1355Combined sources3
Beta strandi1356 – 1359Combined sources4
Turni1363 – 1366Combined sources4
Beta strandi1369 – 1378Combined sources10
Turni1380 – 1385Combined sources6
Beta strandi1387 – 1394Combined sources8
Turni1400 – 1403Combined sources4
Beta strandi1406 – 1409Combined sources4
Beta strandi1417 – 1419Combined sources3
Turni1420 – 1422Combined sources3
Beta strandi1425 – 1428Combined sources4
Helixi1437 – 1440Combined sources4
Helixi1443 – 1445Combined sources3
Beta strandi1446 – 1449Combined sources4
Helixi1456 – 1471Combined sources16
Helixi1474 – 1481Combined sources8
Helixi1483 – 1487Combined sources5
Beta strandi1492 – 1495Combined sources4
Helixi1496 – 1501Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EA0X-ray3.00A/B37-1515[»]
2VDCelectron microscopy9.50A/B/C/D/E/F37-1508[»]
ProteinModelPortaliQ05755.
SMRiQ05755.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05755.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 432Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST396

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

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.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EA0X-ray3.00A/B37-1515[»]
2VDCelectron microscopy9.50A/B/C/D/E/F37-1508[»]
ProteinModelPortaliQ05755.
SMRiQ05755.
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

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_AZOBR
AccessioniPrimary (citable) accession number: Q05755
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 100 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.