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Protein

Ferredoxin-dependent glutamate synthase 2

Gene

gltS

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+.

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 (ferredoxin route).
Proteins known to be involved in this subpathway in this organism are:
  1. Ferredoxin-dependent glutamate synthase 2 (gltS), Ferredoxin-dependent glutamate synthase 1 (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 (ferredoxin 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 bindingi1173Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1179Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1184Iron-sulfur (3Fe-4S)By similarity1

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

Enzyme and pathway databases

BRENDAi1.4.7.1. 382.
UniPathwayiUPA00045.
UPA00634; UER00691.

Protein family/group databases

MEROPSiC44.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin-dependent glutamate synthase 2 (EC:1.4.7.1)
Alternative name(s):
FD-GOGAT
Gene namesi
Name:gltS
Ordered Locus Names:sll1499
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001707941 – 1556Ferredoxin-dependent glutamate synthase 2Add BLAST1556

Interactioni

Protein-protein interaction databases

IntActiP55038. 4 interactors.

Structurei

Secondary structure

11556
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 43Combined sources6
Beta strandi45 – 47Combined sources3
Helixi52 – 63Combined sources12
Helixi64 – 67Combined sources4
Beta strandi74 – 78Combined sources5
Beta strandi80 – 85Combined sources6
Helixi88 – 97Combined sources10
Helixi105 – 107Combined sources3
Beta strandi109 – 115Combined sources7
Helixi119 – 135Combined sources17
Beta strandi139 – 145Combined sources7
Helixi150 – 152Combined sources3
Helixi155 – 160Combined sources6
Beta strandi163 – 170Combined sources8
Helixi177 – 191Combined sources15
Helixi192 – 194Combined sources3
Beta strandi199 – 215Combined sources17
Helixi217 – 219Combined sources3
Helixi220 – 223Combined sources4
Helixi225 – 228Combined sources4
Beta strandi234 – 241Combined sources8
Beta strandi245 – 247Combined sources3
Helixi251 – 253Combined sources3
Beta strandi254 – 256Combined sources3
Beta strandi258 – 264Combined sources7
Helixi269 – 279Combined sources11
Helixi280 – 282Combined sources3
Helixi290 – 296Combined sources7
Helixi306 – 319Combined sources14
Helixi324 – 331Combined sources8
Helixi340 – 342Combined sources3
Helixi346 – 355Combined sources10
Turni356 – 358Combined sources3
Beta strandi364 – 371Combined sources8
Beta strandi373 – 380Combined sources8
Beta strandi389 – 393Combined sources5
Beta strandi398 – 403Combined sources6
Helixi411 – 413Combined sources3
Beta strandi414 – 419Combined sources6
Beta strandi425 – 429Combined sources5
Turni430 – 433Combined sources4
Beta strandi434 – 436Combined sources3
Helixi438 – 446Combined sources9
Helixi451 – 458Combined sources8
Beta strandi459 – 462Combined sources4
Helixi476 – 485Combined sources10
Helixi490 – 495Combined sources6
Helixi497 – 503Combined sources7
Turni518 – 520Combined sources3
Helixi527 – 530Combined sources4
Beta strandi531 – 533Combined sources3
Beta strandi538 – 540Combined sources3
Turni545 – 548Combined sources4
Helixi549 – 551Combined sources3
Beta strandi556 – 559Combined sources4
Beta strandi564 – 566Combined sources3
Helixi569 – 572Combined sources4
Beta strandi574 – 578Combined sources5
Helixi584 – 592Combined sources9
Beta strandi593 – 595Combined sources3
Beta strandi597 – 601Combined sources5
Beta strandi603 – 605Combined sources3
Beta strandi607 – 609Combined sources3
Helixi612 – 628Combined sources17
Beta strandi632 – 639Combined sources8
Helixi640 – 642Combined sources3
Beta strandi646 – 648Combined sources3
Beta strandi649 – 651Combined sources3
Helixi654 – 667Combined sources14
Helixi671 – 673Combined sources3
Beta strandi675 – 679Combined sources5
Helixi686 – 694Combined sources9
Beta strandi698 – 701Combined sources4
Helixi703 – 713Combined sources11
Helixi716 – 722Combined sources7
Turni723 – 725Combined sources3
Helixi732 – 753Combined sources22
Helixi759 – 763Combined sources5
Beta strandi768 – 773Combined sources6
Helixi775 – 781Combined sources7
Helixi794 – 808Combined sources15
Beta strandi809 – 811Combined sources3
Beta strandi820 – 823Combined sources4
Beta strandi826 – 828Combined sources3
Helixi835 – 847Combined sources13
Helixi862 – 871Combined sources10
Helixi878 – 881Combined sources4
Beta strandi882 – 884Combined sources3
Helixi893 – 895Combined sources3
Helixi899 – 903Combined sources5
Turni913 – 915Combined sources3
Helixi918 – 931Combined sources14
Helixi944 – 947Combined sources4
Beta strandi960 – 962Combined sources3
Beta strandi977 – 981Combined sources5
Helixi990 – 995Combined sources6
Beta strandi997 – 1002Combined sources6
Helixi1017 – 1019Combined sources3
Helixi1022 – 1028Combined sources7
Helixi1048 – 1061Combined sources14
Beta strandi1065 – 1072Combined sources8
Helixi1077 – 1086Combined sources10
Beta strandi1090 – 1095Combined sources6
Beta strandi1102 – 1105Combined sources4
Helixi1106 – 1111Combined sources6
Helixi1116 – 1129Combined sources14
Helixi1133 – 1135Combined sources3
Beta strandi1137 – 1143Combined sources7
Helixi1147 – 1155Combined sources9
Beta strandi1159 – 1162Combined sources4
Helixi1165 – 1170Combined sources6
Helixi1179 – 1181Combined sources3
Beta strandi1187 – 1189Combined sources3
Helixi1193 – 1196Combined sources4
Helixi1203 – 1224Combined sources22
Helixi1229 – 1232Combined sources4
Helixi1236 – 1238Combined sources3
Beta strandi1239 – 1241Combined sources3
Beta strandi1248 – 1251Combined sources4
Helixi1256 – 1259Combined sources4
Helixi1269 – 1271Combined sources3
Helixi1283 – 1289Combined sources7
Helixi1291 – 1299Combined sources9
Beta strandi1302 – 1309Combined sources8
Helixi1318 – 1328Combined sources11
Turni1329 – 1331Combined sources3
Beta strandi1336 – 1345Combined sources10
Turni1347 – 1352Combined sources6
Beta strandi1357 – 1365Combined sources9
Turni1369 – 1372Combined sources4
Beta strandi1375 – 1381Combined sources7
Helixi1390 – 1392Combined sources3
Turni1400 – 1403Combined sources4
Beta strandi1408 – 1414Combined sources7
Turni1419 – 1422Combined sources4
Beta strandi1427 – 1431Combined sources5
Turni1437 – 1440Combined sources4
Beta strandi1442 – 1448Combined sources7
Beta strandi1454 – 1456Combined sources3
Turni1457 – 1459Combined sources3
Beta strandi1462 – 1468Combined sources7
Beta strandi1470 – 1472Combined sources3
Helixi1474 – 1477Combined sources4
Turni1480 – 1482Combined sources3
Beta strandi1484 – 1486Combined sources3
Helixi1491 – 1508Combined sources18
Helixi1511 – 1518Combined sources8
Helixi1520 – 1524Combined sources5
Beta strandi1527 – 1531Combined sources5
Turni1533 – 1537Combined sources5
Turni1539 – 1541Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LLWX-ray2.70A37-1556[»]
1LLZX-ray3.00A37-1556[»]
1LM1X-ray2.80A37-1556[»]
1OFDX-ray2.00A/B37-1556[»]
1OFEX-ray2.45A/B37-1556[»]
ProteinModelPortaliP55038.
SMRiP55038.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55038.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 431Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST395

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

HOGENOMiHOG000031558.
InParanoidiP55038.
KOiK00284.
OMAiHGRENDI.
PhylomeDBiP55038.

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.

P55038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFQYPLLAP MTNSSVATNS NQPFLGQPWL VEERDACGVG FIANLRGKPD
60 70 80 90 100
HTLVEQALKA LGCMEHRGGC SADNDSGDGA GVMTAIPREL LAQWFNTRNL
110 120 130 140 150
PMPDGDRLGV GMVFLPQEPS AREVARAYVE EVVRLEKLTV LGWREVPVNS
160 170 180 190 200
DVLGIQAKNN QPHIEQILVT CPEGCAGDEL DRRLYIARSI IGKKLAEDFY
210 220 230 240 250
VCSFSCRTIV YKGMVRSIIL GEFYLDLKNP GYTSNFAVYH RRFSTNTMPK
260 270 280 290 300
WPLAQPMRLL GHNGEINTLL GNINWMAARE KELEVSGWTK AELEALTPIV
310 320 330 340 350
NQANSDSYNL DSALELLVRT GRSPLEAAMI LVPEAYKNQP ALKDYPEISD
360 370 380 390 400
FHDYYSGLQE PWDGPALLVF SDGKIVGAGL DRNGLRPARY CITKDDYIVL
410 420 430 440 450
GSEAGVVDLP EVDIVEKGRL APGQMIAVDL AEQKILKNYQ IKQQAAQKYP
460 470 480 490 500
YGEWIKIQRQ TVASDSFAEK TLFNDAQTVL QQQAAFGYTA EDVEMVVVPM
510 520 530 540 550
ASQGKEPTFC MGDDTPLAVL SHKPRLLYDY FKQRFAQVTN PPIDPLRENL
560 570 580 590 600
VMSLAMFLGK RGNLLEPKAE SARTIKLRSP LVNEVELQAI KTGQLQVAEV
610 620 630 640 650
STLYDLDGVN SLETALDNLV KTAIATVQAG AEILVLTDRP NGAILTENQS
660 670 680 690 700
FIPPLLAVGA VHHHLIRAGL RLKASLIVDT AQCWSTHHFA CLVGYGASAI
710 720 730 740 750
CPYLALESVR QWWLDEKTQK LMENGRLDRI DLPTALKNYR QSVEAGLFKI
760 770 780 790 800
LSKMGISLLA SYHGAQIFEA IGLGAELVEY AFAGTTSRVG GLTIADVAGE
810 820 830 840 850
VMVFHGMAFP EMAKKLENFG FVNYRPGGEY HMNSPEMSKS LHKAVAAYKV
860 870 880 890 900
GGNGNNGEAY DHYELYRQYL KDRPVTALRD LLDFNADQPA ISLEEVESVE
910 920 930 940 950
SIVKRFCTGG MSLGALSREA HETLAIAMNR LGAKSNSGEG GEDVVRYLTL
960 970 980 990 1000
DDVDSEGNSP TLPHLHGLQN GDTANSAIKQ IASGRFGVTP EYLMSGKQLE
1010 1020 1030 1040 1050
IKMAQGAKPG EGGQLPGKKV SEYIAMLRRS KPGVTLISPP PHHDIYSIED
1060 1070 1080 1090 1100
LAQLIYDLHQ INPEAQVSVK LVAEIGIGTI AAGVAKANAD IIQISGHDGG
1110 1120 1130 1140 1150
TGASPLSSIK HAGSPWELGV TEVHRVLMEN QLRDRVLLRA DGGLKTGWDV
1160 1170 1180 1190 1200
VMAALMGAEE YGFGSIAMIA EGCIMARVCH TNNCPVGVAT QQERLRQRFK
1210 1220 1230 1240 1250
GVPGQVVNFF YFIAEEVRSL LAHLGYRSLD DIIGRTDLLK VRSDVQLSKT
1260 1270 1280 1290 1300
QNLTLDCLLN LPDTKQNRQW LNHEPVHSNG PVLDDDILAD PDIQEAINHQ
1310 1320 1330 1340 1350
TTATKTYRLV NTDRTVGTRL SGAIAKKYGN NGFEGNITLN FQGAAGQSFG
1360 1370 1380 1390 1400
AFNLDGMTLH LQGEANDYVG KGMNGGEIVI VPHPQASFAP EDNVIIGNTC
1410 1420 1430 1440 1450
LYGATGGNLY ANGRAGERFA VRNSVGKAVI EGAGDHCCEY MTGGVIVVLG
1460 1470 1480 1490 1500
PVGRNVGAGM TGGLAYFLDE VGDLPEKINP EIITLQRITA SKGEEQLKSL
1510 1520 1530 1540 1550
ITAHVEHTGS PKGKAILANW SDYLGKFWQA VPPSEKDSPE ANGDVSLTGE

KTLTSV
Length:1,556
Mass (Da):169,499
Last modified:November 1, 1997 - v2
Checksum:i4BDAD5F9A4064D9D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti491E → Q in CAA63218 (PubMed:7727752).Curated1
Sequence conflicti570 – 572ESA → NPR in CAA63218 (PubMed:7727752).Curated3
Sequence conflicti642 – 650GAILTENQS → RRNIGLRIKV in CAA63218 (PubMed:7727752).Curated9
Sequence conflicti659G → E in CAA63218 (PubMed:7727752).Curated1
Sequence conflicti940 – 941GG → PP in CAA63218 (PubMed:7727752).Curated2
Sequence conflicti1059H → L in CAA63218 (PubMed:7727752).Curated1
Sequence conflicti1295E → RK in CAA63218 (PubMed:7727752).Curated1
Sequence conflicti1310V → D in CAA63218 (PubMed:7727752).Curated1
Sequence conflicti1323A → S in CAA63218 (PubMed:7727752).Curated1
Sequence conflicti1531Missing in CAA63218 (PubMed:7727752).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92480 Genomic DNA. Translation: CAA63218.1.
D78371 Genomic DNA. Translation: BAA11379.1.
BA000022 Genomic DNA. Translation: BAA18693.1.
PIRiS76781.

Genome annotation databases

EnsemblBacteriaiBAA18693; BAA18693; BAA18693.
KEGGisyn:sll1499.
PATRICi23843556. VBISynSp132158_3309.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92480 Genomic DNA. Translation: CAA63218.1.
D78371 Genomic DNA. Translation: BAA11379.1.
BA000022 Genomic DNA. Translation: BAA18693.1.
PIRiS76781.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LLWX-ray2.70A37-1556[»]
1LLZX-ray3.00A37-1556[»]
1LM1X-ray2.80A37-1556[»]
1OFDX-ray2.00A/B37-1556[»]
1OFEX-ray2.45A/B37-1556[»]
ProteinModelPortaliP55038.
SMRiP55038.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP55038. 4 interactors.

Protein family/group databases

MEROPSiC44.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA18693; BAA18693; BAA18693.
KEGGisyn:sll1499.
PATRICi23843556. VBISynSp132158_3309.

Phylogenomic databases

HOGENOMiHOG000031558.
InParanoidiP55038.
KOiK00284.
OMAiHGRENDI.
PhylomeDBiP55038.

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00691.
BRENDAi1.4.7.1. 382.

Miscellaneous databases

EvolutionaryTraceiP55038.

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 nameiGLTS_SYNY3
AccessioniPrimary (citable) accession number: P55038
Secondary accession number(s): Q59980
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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
  4. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.