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
//