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Protein

Ferredoxin-dependent glutamate synthase

Gene

gltB

Organism
Antithamnion sp. (Red alga)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 (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 sitei27For GATase activityBy similarity1
Metal bindingi1158Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1164Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1169Iron-sulfur (3Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1105 – 1162FMNBy similarityAdd BLAST58

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

UniPathwayiUPA00045.
UPA00634; UER00691.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin-dependent glutamate synthase (EC:1.4.7.1)
Alternative name(s):
Fd-GOGAT
Gene namesi
Name:gltB
Synonyms:glsF
Encoded oniPlastid; Chloroplast
OrganismiAntithamnion sp. (Red alga)
Taxonomic identifieri2767 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaFlorideophyceaeCeramialesCeramiaceaeAntithamnion

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001707901 – 1536Ferredoxin-dependent glutamate synthaseAdd BLAST1536

Proteomic databases

PRIDEiQ06434.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliQ06434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 427Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST401

Sequence similaritiesi

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

Keywords - Domaini

Glutamine amidotransferase

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.

Q06434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVSKYFTHQ LSQFSGYPSI VSERDACGVG FIANLNSKPS NKIVTEALNA
60 70 80 90 100
LSCMEHRGGC GADNISGDGA GVTIQIPWDI FISEGINFLP KLQSNQSILN
110 120 130 140 150
YGVRMILRSS DDLDKIKKIF SWALDEYQLD LISWRNVPVD KSILGEESKF
160 170 180 190 200
NQPLVVQCIV RSNNLIDYKL DKHLYLVRKK IEKLVSKLDI NTNKQFYICS
210 220 230 240 250
FSSKTIVYKG MLRSEFLVKY YNDLSNSLYV SNFAMYHRRF STNTMPKWSL
260 270 280 290 300
AQPMRFMAHN GEINTLLGNL NWNKSKESLL KSSIWSDYYD ILSPITNLEN
310 320 330 340 350
SDSANLDSVL ELFIHSGRTP QEALMILIPE AYKNQPALSL FPEITDFYEY
360 370 380 390 400
YSILQEPWDG PALVVFTDGK FVGATLDRNG LRPARYTITD DGFISLSSET
410 420 430 440 450
GVSNINSQNV VTKGRLGPGQ MLCVDLSKNL VLDNWMIKQQ ISQKFPYKEW
460 470 480 490 500
VNKYQSNLNL LEYLNDFTFD KVQMNRWHTA FGYTNEDVEL VIEHMASSAK
510 520 530 540 550
EPTFSMGDDT PLPILSEKPH LIYDYFKQRF AQVTNPAIDP LRESLVMSLI
560 570 580 590 600
TYLGPKGNIL EPTAIMAKSI KLESPIINEN ELAQLNSFNL SVVTVPTFID
610 620 630 640 650
KHLSTQTFVD KILEICSQCD SYISQGIEIL VLSDRIEILP VDKIFVSPLL
660 670 680 690 700
IVGAVHHYLI KKQLRHKVSL VIDTGQCWTT HHFALLIGYG ASAICPYLAF
710 720 730 740 750
LTVRQWWHNS RTQKLMSTGK LSRLTIQESQ DNYRSAIEKG LLKILSKMGI
760 770 780 790 800
SLLSSYHGAQ IFEILGLGQD VVDLAFSGTV SRLNGMTLNE LYEDSLKSYN
810 820 830 840 850
LAFITEIPKK LPNLGYVQYR PSAEYHVNNP EMSKTLHKAV RNNDNILYSK
860 870 880 890 900
YKSLLNDRRP TNLRDLLELK TDRQPISIDQ VEDVNSVLMR FCTGGMSLGA
910 920 930 940 950
LSRETHETLA IRMNRIGGKS NSGEGGEDST RFKSIQDLDT SGVSRTFSHL
960 970 980 990 1000
KGLKINDLAS SAIKQIASGR FGVTPEYLVN AKQLEIKIAQ GAKPGEGGQL
1010 1020 1030 1040 1050
PGKKVSPYIA ELRNCKPGVT LISPPPHHDI YSIEDLAQLI FDLHQINPDA
1060 1070 1080 1090 1100
QVSVKLVASL GIGTIAAGVA KGNADIIQIS GHDGGTGASP LSSIKHAGAP
1110 1120 1130 1140 1150
WDVGLAEVHT TLVENSLREK VILRVDGGLR TGKDIIIAAL MGAEEFGFGT
1160 1170 1180 1190 1200
VAMIATGCVM ARVCHTNNCP VGVATQRQDL RNRFPGIPSD VVNFFIFVAE
1210 1220 1230 1240 1250
EVREILAELG YKSLEELIGL NDLFKVKDIE LSKTKNLNLN ILFNSINMNR
1260 1270 1280 1290 1300
NLIPKLKHKT VHTNGNVLDD ILLSKSNIIN AINLQSNIVQ DIEILNTDRC
1310 1320 1330 1340 1350
VGARISGLIT KMYGRDNFNG NLQLNFVGSA GQSFGAFISK GIHLYLKGEA
1360 1370 1380 1390 1400
NDYVGKGMNG GEIIICPPIE QKTSSSNQVI LGNTCLYGAT GGYLFANGQA
1410 1420 1430 1440 1450
GERFAVRNSN GYSVVEGVGD HACEYMTGGL IVVLGTFGRN IGAGMTGGIA
1460 1470 1480 1490 1500
YFLDEDNTLK NKLNTEIVKA QRLLTKESEE QLKNIMELYE IKTKSEKAKL
1510 1520 1530
ILDNWSQYLA KFYQIVPPSE QIQHLLMLIF FFSKYC
Length:1,536
Mass (Da):171,112
Last modified:June 1, 1994 - v1
Checksum:iE803CED3004F321C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21705 Genomic DNA. Translation: CAA79809.1.
PIRiS39510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21705 Genomic DNA. Translation: CAA79809.1.
PIRiS39510.

3D structure databases

ProteinModelPortaliQ06434.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ06434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00691.

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_ANTSP
AccessioniPrimary (citable) accession number: Q06434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 5, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.