UniProt: A0LTU0

Database: UniProt
Entry: A0LTU0_ACIC1

LinkDB:  A0LTU0_ACIC1 
Original site:  A0LTU0_ACIC1

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (7)   
   Pfam (4)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   A0LTU0_ACIC1            Unreviewed;      1513 AA.
AC   A0LTU0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:ABK52850.1};
DE            EC=1.4.1.14 {ECO:0000313|EMBL:ABK52850.1};
GN   OrderedLocusNames=Acel_1078 {ECO:0000313|EMBL:ABK52850.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52850.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK52850.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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; CP000481; ABK52850.1; -; Genomic_DNA.
DR   STRING; 351607.Acel_1078; -.
DR   MEROPS; C44.003; -.
DR   KEGG; ace:Acel_1078; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_11; -.
DR   InParanoid; A0LTU0; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016040; F:glutamate synthase (NADH) 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   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:ABK52850.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221}.
FT   DOMAIN          31..418
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1513 AA;  164691 MW;  D0C5AC9EDC428871 CRC64;
     MSTSPISPVD LGLPDPTPRG LYDPRFDRDS CGVAFVADLR RGPSHSVIEL ALTALRNLEH
     RGATGREADT GDGAGLLAQI PDAFFRAILD VDLPPAGGYA AGIAFLPTDN FAAATKVSAI
     ERIVAEEQLR VLAWRELPID PSVPGPSARA VMPRFRQLFV APVDSSLTGI DVERRTFRAR
     KRIEREVGVY FPSLSPRTIV YKGMLTAPQL ERFFPDLADP RFASALALVH SRFSTNTFPS
     WPLAHPYRYI AHNGEINTIM GNRNWMRARE TLLASDRIPG DLSQLFPIIT PGGSDSMSFD
     EVLELLHLGG RSLPHAVLMM IPEAWENNDE MPDDLRAFYE FHASVMEPWD GPACVTFTDG
     TVIGAVLDRN GLRPGRYWVT EDGLVVLASE VGVLDIDPAT VIRKGRLQPG RIFLVDLSQG
     RIIDDAEIKA QLAAEKPYRE WLHAGLLKLP DLPDREHVVY THESVLRRQQ TFGYTEEELR
     LILAPMARSG AEPIGSMGND APLAVLSNRP RLLFDYFTQL FAQVTNPPLD AIREELVTSL
     ANTIGPEQNL LEPTPASCRQ IVVPFPVIDN DELAKILHIN DDGDLPGLAP YVVRGLYRVS
     GGGAALRERL AEICAEVSEA IERGARIIVL SDRDSDREFA PIPSLLLTGA VHHHLIREKT
     RTKVGLVVEA GDVREVHHVA LLIGYGAAAV NPYLAMETVE DMVRTGFLRG IDAQTAVHNL
     VKALGKGVLK VMSKMGISTV ASYTGAQVFE ALGLSQEVID RYFTGTPSKL GGVGLDVLAE
     EVAARHRKAY PVDEVRPSHR RLDVGGDYQW RREGELHLFN PETVFRLQHS TRTGRYDIFK
     QYTRLVDEQS RNLMTLRGLF RLRTGVRPPV PIEEVEPVSS IVKRFSTGAM SYGSISQEAH
     ETLAIAMNRL GAKSNTGEGG EDPERLYDER RSAIKQVASG RFGVTAEYLT AADDLQIKMA
     QGAKPGEGGQ LPGHKVYPWI AKTRYSTPGV GLISPPPHHD IYSIEDLKQL IHDLKNANPR
     ARIHVKLVAE TGVGTVAAGV AKAKADVVLI SGHDGGTGAS PLTSIKHAGA PWELGLAETQ
     QTLVANGLRD RIVVQTDGQL KTGRDVIIAA LLGAEEFGFA TAPLVVSGCI MMRVCHLDTC
     PVGVATQNPE LRKRFNGKPE FVINFFEFIA QEVREYLAAL GFRSLDEAIG QVEFLDVSDA
     IDHWKASGLD LSPILRVPDN RDEPRRCVTV QDHGLDKALD NTLIALCEGA LNDATPVKLE
     LPIRNVNRTV GTMLGHEVTK RYRGAGLPDD TIDITFTGSA GQSFGAFLPR GITLRLIGDA
     NDYVGKGLSG GRIILRPPLE APFEAHKNII AGNVMFYGAT AGEGFVRGVV GERFCVRNSG
     VTAVVEGVGD HGCEYMTGGV VVVLGATGRN FAAGMSGGVA YVLDLDPLRV NTEMVDLDPL
     DSDDAEVLER LVRKHAAETG STVAAELLAD WPAALARFTK IMPQDYKRVL AAKALAEQTG
     ADVNEQIMAA AHG
//

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