UniProt: D4GUL6

Database: UniProt
Entry: D4GUL6_HALVD

LinkDB:  D4GUL6_HALVD 
Original site:  D4GUL6_HALVD

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (7)   
   Pfam (4)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (24)   

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ID   D4GUL6_HALVD            Unreviewed;      1511 AA.
AC   D4GUL6; L9UQF7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ADE02856.1};
DE            EC=1.4.7.1 {ECO:0000313|EMBL:ADE02856.1};
GN   Name=gltB {ECO:0000313|EMBL:ADE02856.1};
GN   OrderedLocusNames=HVO_0869 {ECO:0000313|EMBL:ADE02856.1};
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE02856.1, ECO:0000313|Proteomes:UP000008243};
RN   [1] {ECO:0000313|EMBL:ADE02856.1, ECO:0000313|Proteomes:UP000008243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|ARBA:ARBA00001927};
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716}.
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DR   EMBL; CP001956; ADE02856.1; -; Genomic_DNA.
DR   RefSeq; WP_004044068.1; NZ_AOHU01000096.1.
DR   STRING; 309800.HVO_0869; -.
DR   MEROPS; C44.003; -.
DR   PaxDb; 309800-C498_14393; -.
DR   EnsemblBacteria; ADE02856; ADE02856; HVO_0869.
DR   GeneID; 8924045; -.
DR   KEGG; hvo:HVO_0869; -.
DR   PATRIC; fig|309800.29.peg.2771; -.
DR   eggNOG; arCOG04553; Archaea.
DR   HOGENOM; CLU_000422_8_2_2; -.
DR   OrthoDB; 211693at2157; -.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00982; gltB_C; 1.
DR   CDD; cd00713; GltS; 1.
DR   CDD; cd02808; GltS_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR002489; Glu_synth_asu_C.
DR   InterPro; IPR036485; Glu_synth_asu_C_sf.
DR   InterPro; IPR006982; Glu_synth_centr_N.
DR   InterPro; IPR002932; Glu_synthdom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 1.
DR   Pfam; PF00310; GATase_2; 1.
DR   Pfam; PF04898; Glu_syn_central; 1.
DR   Pfam; PF01645; Glu_synthase; 1.
DR   Pfam; PF01493; GXGXG; 1.
DR   SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ADE02856.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008243}.
FT   DOMAIN          25..418
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1511 AA;  163908 MW;  A952F7C359215C1A CRC64;
     MTKPHIDAPF AQDGLADPTD ERSNCGVGAV VDLENGASHR VVADSLELLE NLEHRGTTGA
     EENTGDGAGI LLQRPDEFFE AVLESELPDL YAAGSVFMPT DDEVRERVSA VVEDSLADHG
     LSVFDWRDVP TDNADLGATA LESEPDVWQL FVEPADGMTV DEFDRALYLA RRAAEKAVDD
     LAIEGAGRFY VCSLDRKTIV YKGLLTAEQL PNYYPDLSDE RMVTELALVH ARFSTNTLGA
     WHLAHPYRQV IHNGEINTIR GNVNWMRARE TDLQHEAFGD DIETLMPITK ADQSDTASVD
     NVVELLLKSG RELPHVLRML IPEAYRNDDA MDQARRDWYD FHASLVEPWD GPALVAATDG
     DRIAAVLDRN GLRPCRYEVT TDGRLIVASE VGALDTDPAE LESRGRLQPG EIFMADPEEG
     RVIPDAEVFD SLTDEKYGEW VDQQQRHLDD IAGDTDSTSR GQVESLRATQ AAFGYTHDQL
     NHMIEPMARD GKDPVGSMGD DTPLSVLSDL NRPLFTYFKQ LFAQVSNPPI DYIREKLVTS
     LESRLGRQRN LLDESPEHAR QLVLDSPVLT DAETAAIKDL DDDIRSEVVD ITYEKGGDIR
     EAIEAVRDEA KAVIEDGADI VVLSDRAVGP DRVAIPSLLA TGAVHHSLVR NGLRNHAGLV
     VESGDPREVH HLATLVGYGA GAVNPYLAYQ TIEDVVTGPD GADEGEAIDA YVHALEDGLL
     KTMAKMGIST VESYRGAQIF EAVGLESDFV AEYFEGTEIR TEGIGLDVIE EDLLTRHAAA
     FGADPKLERQ GEYENRSAGI HHGWNPQTVG TLQQSVRAGD YEKYKEFAEL VNDQSKQLKA
     LRGLLEFDSD REPVDIDEVE PVEDIVKRFS TAAMSLGSLS PEAHENNSIA MNRIGGKSNS
     GEGGEPPERF GTEKECNVKQ VASGRFGVTS HYLSSADEIQ IKMAQGSKPG EGGHLPGKKV
     NEMIAHVRYA TPGVGLISPP PLHDIYSIED LKQLIFDLKS ANPDADINVK LVSEAGIGTI
     AAGVSKAKAD VVHISGYDGG TGASPKTSIK NAGLPWELGL AEANQMLRAT GLRSRIRVSV
     DGGMKTGRDV AVAALLGGEE YVFGTASLVT SGCVMARQCH ENTCPVGVAT QDENLRRRFP
     GEPDHVINYM TFIAQELREI MADLGFTSLD EMIGRLSLLR QVETDHEKAK HLDLSSVLAE
     PETGARRKTE AQVHADIETH VDHKLIDEAA DAIENREPVV IRRDLSNVDR AVGAMLSNRI
     SNAHGGEGLP DDTIRCEFDG IAGQTFGGFL ARGVTMRLTG AANDYVGKGL SGGRVIVDTP
     AEANYEAAEN ILIGNVALYG ATQGECYVNG LAGERFGVRN SGVKAVVEGV GDHGCEYMTG
     GVVAVLGETG RNFAAGMSGG VAYVYDPDDE FAAKANTEMV TLEDHLDDKD EAMLTRLVEN
     HRTYTDSDRA AELLDDWQSV LGDFVKVMPD AYAEVIAEDG REDVRNELPA KAGAIVDAGA
     DRVGAATTSD D
//

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