ID A0A147HBJ4_9BURK Unreviewed; 1578 AA.
AC A0A147HBJ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KTT27332.1};
GN ORFNames=NS331_02565 {ECO:0000313|EMBL:KTT27332.1};
OS Pseudacidovorax intermedius.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pseudacidovorax.
OX NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT27332.1, ECO:0000313|Proteomes:UP000072741};
RN [1] {ECO:0000313|EMBL:KTT27332.1, ECO:0000313|Proteomes:UP000072741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS331 {ECO:0000313|EMBL:KTT27332.1,
RC ECO:0000313|Proteomes:UP000072741};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTT27332.1}.
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DR EMBL; LDSL01000018; KTT27332.1; -; Genomic_DNA.
DR RefSeq; WP_058640445.1; NZ_LDSL01000018.1.
DR PATRIC; fig|433924.3.peg.1787; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000072741; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000072741}.
FT DOMAIN 25..425
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1578 AA; 172098 MW; E414C9413FD508F1 CRC64;
MTLAAEIEHL QQKGLYVTAN EHDACGVGFV AHIKGEKRHD IVTQALKILE NIDHRGAVGA
DKLMGDGAGI LLQIPDALYR EEMAKQGVTL PPAGEYGVGM IFLPKEHASR LACEQEMERA
IKAEGQVLLG WRDVPVNREM PMSPTVRDKE PVMRQVFIGR GADVIVQDAL ERKLYVIRKT
ASANIQALKL KHSKEYYVPS MSSRTVVYKG LLLADQVGTY YLDLQDARCI SAIGLVHQRF
STNTFPEWPL AHPYRYVAHN GEINTVKGNY NWMRAREGVM SSPVLGADLA KLYPISFAGQ
SDTATFDNCL ELLTMAGYPI SQAVMMMIPE PWEQHATMDP RRRAFYEYHA AMLEPWDGPA
AVVFTDGKQI GATLDRNGLR PARYCVTDDD MVIMGSEAGV LPIPEAKIIR KWRLQPGKMF
LIDLDQGRMI DDEEVKATLA HSKPYKQWIE NLRIKLDDVE GAGEAPASPV SLLDRQQAFG
YTQEDIKFLM SPMAVAGEEG IGSMGNDSPL AVLSSKNKPL YNYFKQLFAQ VTNPPIDPIR
EAIVMSLVSF VGPKPNLLDI NQVNPPMRLE VSQPVLDFND MAKLRDIGTF TQGKFKSYTL
DITYPLAWGE EGVEAKLASL CAEAVDAIKG GHNILIVSDR AMSAEQLPIP AVLALSAIHQ
HLIREGVRTS AGLVVETGSA REVHHFAVLA GYGAEAVHPY LAMETLAAMH QDLPVDMSAE
KAIYNYVKAI GKGLSKIMSK MGVSTYMSYC GAQLFEAIGL NTETVNKYFT GTASRVEGIG
VFEIAQEAIR MHKAAFGDDP VLESMLDAGG EYAWRTRGED HMWTPDAIAK LQHSTRANNF
NTYKEYAQII NDQSRRHLTL RGLFEFKFDA AKAIPVDEVE SAADIVKRFA TGAMSLGSIS
TEAHSTLAIA MNRIGGKSNT GEGGEDPARY RNELKGIAIK QGATLKSEIG AQNVEVDLPL
KEGDSLRSRI KQVASGRFGV TAEYLASSDQ IQIKMAQGAK PGEGGQLPGG KVTEYIGKQR
YSVPGVGLIS PPPHHDIYSI EDLAQLIHDL KNVAPHASIS VKLVSEVGVG TIAAGVAKCK
SDHVVIAGHD GGTGASPWSS IKHAGSPWEI GLAETQQTLV LNRLRGRIRV QADGQMKTGR
DVVIGALLGA DEFGFATAPL VVEGCIMMRK CHLNTCPVGV ATQDPVLRRK FAGKPEHVVN
YFFFVAEEVR QIMAQLGVRK FDELIGRAEL LDMRKGIAHW KARGLDFSRL FAQPQVPAEV
PRLHVDSQEH GLEKSLDNKL IEKSRPAIDR GEKVQFIETV RNVNRSVGAM LSGALTKVHP
EGLPDDSIRI QLEGTGGQSF GAFLARGITL YLIGEANDYT GKGLSGGRVV VRPSLDFRGE
AARNIIVGNT ALYGATTGEA FLAGVAGERF AVRLSGATAV VEGTGDHGCE YMTGGTVVVL
GKTGRNFAAG MSGGVAFVYD EDGQFASRCN LAMVTLDKVL TTGEQTAGID RKFWHNAQTD
EAQLRKLLEE HHRWTGSKRA RDLLDDWALS RTKFVKVFPN EYKRALGEIH DRKMMLASTG
NDAKAGLEPH AVSAAAAG
//
