UniProt: A0A0L7T7F8

Database: UniProt
Entry: A0A0L7T7F8_9GAMM

LinkDB:  A0A0L7T7F8_9GAMM 
Original site:  A0A0L7T7F8_9GAMM

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Ontology (5)   
   GO (5)   
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 (20)   

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ID   A0A0L7T7F8_9GAMM        Unreviewed;      1843 AA.
AC   A0A0L7T7F8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=GltA {ECO:0000313|EMBL:KOC91290.1};
GN   ORFNames=NG42_05435 {ECO:0000313|EMBL:KOC91290.1};
OS   Winslowiella iniecta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Winslowiella.
OX   NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC91290.1, ECO:0000313|Proteomes:UP000037088};
RN   [1] {ECO:0000313|EMBL:KOC91290.1, ECO:0000313|Proteomes:UP000037088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B120 {ECO:0000313|EMBL:KOC91290.1,
RC   ECO:0000313|Proteomes:UP000037088};
RX   PubMed=26198254;
RA   Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA   Tisserat N.A., Leach J.E.;
RT   "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT   noxia).";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOC91290.1}.
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DR   EMBL; JRXE01000006; KOC91290.1; -; Genomic_DNA.
DR   RefSeq; WP_052898254.1; NZ_JRXE01000006.1.
DR   PATRIC; fig|1560201.3.peg.1164; -.
DR   Proteomes; UP000037088; Unassembled WGS sequence.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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   Reference proteome {ECO:0000313|Proteomes:UP000037088}.
FT   DOMAIN          21..403
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   COILED          588..615
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1843 AA;  200634 MW;  A641C0BD706C5F73 CRC64;
     MSNQTPYPYG LYDPSKESDS CGVGFITRKD GEQTHEILQM AHSALCTVPH RGGMSAEGVG
     DGAGVNVDIS LHFFRKITGQ PLEFGRFGVG NFFVPKDPAL RANAERLVEE TFAVYGFPII
     VKRDLPLDAS VLRPAAIQFQ LPIVQWVFAA PQDVDDQNGF EQRIYRALLD IESRAFTESE
     FGGLYPLSLS SRTQVLKARL NSNEVIPYFK DLTDSDHQVR GLFFHTRFST NTDPHTTMAQ
     PFRLMAHNGE LNTDRKNRIA EAALALARGK KIVRPKGQSD SSRLDQSIHS RLMEDNLDLI
     NAVVSMMPPA WENDDSLSDN VRAMLEYFSL YEEKNDGPAA LIFGNGDIIG ARLDRLGLRP
     LRSVETAEYI GAMSEAGQIA FPPESVLRRG RIEAGGMLYY DHSEKRSYTT LEALEKLAAE
     KDYPALLEQA RVTLGDLPVV PAEQQGSPLR YSGDLKAYQR FVAYYYNQES FKFMMDPMLS
     TGAEKISAMG YGNAINGLSD HEGGMAHYFS QRFAQVTNPP LDSIREADGM TLRVALGAKP
     HLGRSKGQQI IVPTPILTHL DMLQLREQKV APYARFEMLY QPIIGTDAQS RQDNARALEN
     AIDDLAQQVV EFARAQGGIA VITDRHISST RAAMPMLLVV SAINQRLVQE GLRLDVSLVV
     ESGQSISSHH IAATLGFGAS AIYPLGVQMR AEEKYGEGEE GNKAFKRYAK AAEKALMKTM
     GKVGLCTVES YSCGEFFEPN FLDTDDAVLK KYFPNIKTPV GGASFATIAQ MAVDWHQSAL
     KIKGESEVPL LGLFKERAEG AGHSYGTIAV RTFIDMTEQP IRFADKPRED DQFIRLLTLA
     RLDNAFNIKA KSFADSSFER IPDEVIDNFT ITPDYRQFSS LMHEERKRRP AALRDILAFP
     ADLTHVDSLA EFSRKLSRYS LINNGFAIRG LVCETHADNA GLFTLRLTDA IEGLKPEAER
     LAALSTALKN RFAADIAHTE MVAGGLQVSA HGKAADYLAR IFTTSPSLPL SEVQPASEIT
     RTFASGAMSH GALVAPAHEA VAHGTNMVGG MSNCGEGGEH YSRHGTIRAS RIKQLASGRF
     GVWAAYLADP MLEELEIKIG QGAKPGEGGQ LPSAKVTVEI AAARGGTPGV ELVSPPPHHD
     TYSIEDLAQL IHDCKAARVR VIVKLVSSEG IGTIAVGVAK AGADVINVAG NTGGTGAASV
     TSLKYTGRVA EIGIAEVHQA LCANGLREKV ILRCSGAQQT GSDVVKSALL GGDSFEFGTT
     ALMMLKCVMA KNCNVKCPAG LTTNAEAFDG DPRQLAQYFI NVAHEVREML ARLGLRSLRE
     ARGRSELLHL MDHPREVGKL DLRAMLTVVP EQKIAHPVYL EKDFALDEGW LARLNGSLVA
     QGAAHIQLGD GITLNNRHKS VGGQLAIDIE RMLNHQLDDA QLQTMPAALS DDRGRRYLAP
     ATVTISTSGS AGQSYGVFCN DGMQLTHSGT CNDGVGKGQC GGEIIVRSPG GGSQDTDGNV
     LIGNFALFGA TGGRLFVQGQ AGDRFAVRNS GATAVVEGVG DFCCEYMTNG AILNLGTFGK
     GFGNGMSGGF AYQYDPYGTL AAHAAGDSVL FGSIADDDEM AKVHKQAVLT MLNWHLEATG
     SERAAWLLEH WETECQHFVF VMPRSLLLYQ DSVEILKAKT RKDLLEELST ALASHQVTKF
     KNAWRNRTTI ANGAVPSYGA TDTPEMFVLL NNYTVLSTVQ QLALSRLPKG TSVEDPAVEK
     AVRNLLMTED FALISKLQRH ARSAIENYSD EELSCLIAAK RMADYKAALT QRNIRSMDSL
     ATYGWIIYQD ARNREVLGRL PDFEELFARA ALPELAAAVG KLS
//

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