ID K0HXT9_9BURK Unreviewed; 1577 AA.
AC K0HXT9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:AFU44585.1};
GN ORFNames=C380_04330 {ECO:0000313|EMBL:AFU44585.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU44585.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU44585.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU44585.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
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; CP003872; AFU44585.1; -; Genomic_DNA.
DR RefSeq; WP_015012667.1; NC_018708.1.
DR STRING; 358220.C380_04330; -.
DR KEGG; ack:C380_04330; -.
DR PATRIC; fig|358220.3.peg.887; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_4; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000006306; Chromosome.
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 25..425
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 326..361
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
SQ SEQUENCE 1577 AA; 172402 MW; 363448511B43FAF6 CRC64;
MTTAAEIQHL QQHGLYSSGN EHDACGLGFV AHIKGIKRHD IVTQALKILE NIDHRGAVGA
DPLMGDGAGI LIQIPDALYR EEMAKQGVTL PAAGEYGVGM IFLPKEHASR LACEQEMERA
IKAEGQVLLG WRDVPVNVDM PMSPTVRKKE PILRQVFIGR GNDVIVQDAL ERKLYVIRKT
ASANIQALKL KHSKEYYVPS MSSRTVVYKG LLLADQVGVY YKDLSDERCV SAIGLVHQRF
STNTFPEWPL AHPYRYVAHN GEINTVKGNY NWMKAREGVM ASPVLAADLQ KLYPISFADQ
SDTATFDNCL ELLTMAGYPI SQAVMMMIPE PWEQHTTMDE RRRAFYEYHA AMLEPWDGPA
SIVFTDGRQI GATLDRNGLR PSRYCITDDD LVIMGSESGV LPVPENKIVR KWRLQPGKMF
LIDLEQGRMI DDDELKANIV NTKPYKQWIE NLRIKLDSIE AGAQAAAPHA ADLPLLDRQQ
AFGYTQEDIK FLMAPMAKNG EEGIGSMGND SPLAVLSGKN KPLYNYFKQL FAQVTNPPID
PIREAIVMSL NSFIGPKPNL LDINQVNPPM RLEVSQPVLD FADMAKLRDI EKYTQGKFKS
ATIDITYPLS WGREGVEAKL ASLCAQAVDA IKGGANILII SDRAVSATQV AIPALLALSA
IHQHLVGAGL RTTAGLVVET GTAREVHHFA VLAGYGAEAV HPYLAMETLA EMHKDLGGDL
SADKAIYNYV KAIGKGLSKI MSKMGVSTYM SYCGAQLFEA IGLNTETVAK YFTGTASRVE
GIGVFEIAEE AIRMHKAAFG DDPVLETMLD AGGEYAWRAR GEDHMWTPDA IAKLQHSTRA
NNWNTYKEYA QIINDQSKRH MTLRGLFEFK IDPSKAISID EVEPAKEIVK RFATGAMSLG
SISTEAHATL AVAMNRIGGK SNTGEGGEDA ARYRNELKGI PIKKGDSLKS VIGAENVEVD
LPLQDGDSLR SRIKQVASGR FGVTAEYLSS ADQIQIKMAQ GAKPGEGGQL PGGKVSNYIG
KLRHSVPGVG LISPPPHHDI YSIEDLAQLI HDLKNVAPHA GISVKLVSEV GVGTIAAGVA
KCKSDHVVIA GHDGGTGASP WSSIKHAGGP WEIGLAETQQ TLVLNRLRGR IRVQADGQMK
TGRDVAIGAL LGADEFGFAT APLVVEGCIM MRKCHLNTCP VGVATQDPEL RKKFSGKPEH
VVNYFFFIAE EVRQIMAQLG IRKFDDLIGR TDLLDMRQGL EHWKARGLDF SRLFAQPNVP
ADVPRFHVDV QDHNIEHTLD RKLIERSKPA IEKGERVQFI EVARNVNRSV GAMLSGAVTR
VHPEGLPDDT IRIQLEGTGG QSFGAFLTRG ITLYLIGDAN DYTGKGLSGG RVIVRPSIDF
RGEAVRNTIV GNTVMYGATT GEAFFSGVAG ERFAVRLSGA TAVVEGTGDH GCEYMTGGTV
VVLGKTGRNF AAGMSGGVAY VYDEDGQFDT RCNLSMVTLE RILPATEQEA TVPRSIWHNG
QTDEAQLKKL LEDHNRWTGS KRARELLDNW AASRSKFVKV FPTEYKRALA EIYERKVLEE
SATPAVAATK KEVAPAK
//
