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Database: UniProt
Entry: A0A0Q4R8U9_9BURK
LinkDB: A0A0Q4R8U9_9BURK
Original site: A0A0Q4R8U9_9BURK 
ID   A0A0Q4R8U9_9BURK        Unreviewed;      1577 AA.
AC   A0A0Q4R8U9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KQO14907.1};
GN   ORFNames=ASF16_18050 {ECO:0000313|EMBL:KQO14907.1};
OS   Acidovorax sp. Leaf78.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1736237 {ECO:0000313|EMBL:KQO14907.1, ECO:0000313|Proteomes:UP000051234};
RN   [1] {ECO:0000313|Proteomes:UP000051234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQO14907.1}.
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DR   EMBL; LMLZ01000025; KQO14907.1; -; Genomic_DNA.
DR   RefSeq; WP_056173445.1; NZ_LMLZ01000025.1.
DR   STRING; 1736237.ASF16_18050; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000051234; 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; 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   InterPro; IPR001202; WW_dom.
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.
DR   PROSITE; PS50020; WW_DOMAIN_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}.
FT   DOMAIN          26..426
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          327..362
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
SQ   SEQUENCE   1577 AA;  172119 MW;  D43116048D24C5AA CRC64;
     MTTTAAEIEH LQQHGLYSSG NEHDACGLGF VAHIKGVKRH DIVTQALKIL ENIDHRGAVG
     ADPLMGDGAG ILIQIPDALY REEMAKLGVT LPAAGEYGVG MIFLPKEHAS RLACEQEMER
     AIKAEGQVLL GWRDVPVNLD MPMSPTVRKK EPILRQVFIG RGNDVIVQDA LERKLYVIRK
     TASAAIQNLK LKHSKEYYVP SMSSRTVVYK GLLLADQVGV YYKDLSDERC VSAIGLVHQR
     FSTNTFPEWP LAHPYRYVAH NGEINTVKGN YNWMKAREGV MASPVLAADL QKLYPISFAD
     QSDTATFDNC LELLTMAGYP ISQAVMMMIP EPWEQHTTMD ERRRAFYEYH AAMLEPWDGP
     ASIVFTDGRQ IGATLDRNGL RPSRYCITDD DLVIMGSESG VLPIPENKIV RKWRLQPGKM
     FLIDLEQGRM IDDDELKANV VNTKPYKQWI ENLRIKLDSV GTDTASTPDA APLPLLDRQQ
     AFGYTQEDIK FLMAPMAKNG EEGIGSMGND SPLAVLSGKN KPLYNYFKQL FAQVTNPPID
     PIREAIVMSL VSFIGPKPNL LDINQVNPPM RLEVSQPVLD FADMAKLRNI EKYTQGKFKS
     ATIDITYPLS WGREGVEAKL ASLCAQAVDA IKGGANILIV SDRAVSATQV AIPALLALSA
     IHQHLVGAGL RTTAGLVVET GTAREVHHFA VLGGYGAEAV HPYLAMETLA EMHKDMPGDL
     SPDKAIYNYV KAIGKGLSKI MSKMGVSTYM SYCGAQLFEA IGLNTDTVGK YFTGTASRVE
     GIGVFEIAEE AIRMHKAAFS DDPVLETMLD AGGEYAWRTR GEDHMWTPDA IAKLQHSTRA
     NNWNTYKEYA QIINDQSKRH LTLRGLFEFK IDPSKAISID EVEPAKEIVK RFATGAMSLG
     SISTEAHATL AVAMNRIGGK SNTGEGGEDA ARYRNELKGI PIKQGDTLKS VIGAANVEVD
     LPLQDGDSLR SKIKQVASGR FGVTAEYLSS ADQIQIKMAQ GAKPGEGGQL PGGKVSNYIG
     KLRHSVPGVG LISPPPHHDI YSIEDLAQLI HDLKNVAPHA TISTKLVSEV GVGTIAAGVT
     KCKSDHLVIA GHDGGTGASP WSSIKHAGGP WEIGLAETQQ TLVLNRLRGR VRVQADGQMK
     TGRDVAIGAL LGADEFGFAT APLVVEGCIM MRKCHLNTCP VGVATQDPEL RKKFSGKPEH
     VVNYFFFIAE EVRQIMAQLG IKKFDDLIGR SDLLDTRSGI AHWKARGLDF GRLFAQPNVP
     ADVPRYHVDV QDHNITNTLD RKLIERSKPA IDKGERVQFI EVARNVNRSV GAMLSGAVTR
     VHPEGLPDDT IRIQLEGTGG QSFGAFLTRG ITLYLIGDAN DYTGKGLSGG RVIVRPSIDF
     RGESVRNTIV GNTVMYGATT GEAFFSGVAG ERFAVRLSGA TAVVEGTGDH GCEYMTGGTV
     VVLGKTGRNF AAGMSGGVAY VYDEDGQFDT RCNMSMVTLE RILPASEQEA TMPRAIWHGG
     QSDEAQLKKL LEDHNRWTGS KRARELLDNW AASRGKFVKV FPTEYKRALA EIYERKVLEE
     PATPAVAAPE KVAVPAK
//
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