ID W1DN93_KLEPN Unreviewed; 894 AA.
AC W1DN93;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glutamate synthase [NADPH] large chain {ECO:0000313|EMBL:CDL09594.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:CDL09594.1};
OS Klebsiella pneumoniae IS43.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL09594.1, ECO:0000313|Proteomes:UP000019183};
RN [1] {ECO:0000313|EMBL:CDL09594.1, ECO:0000313|Proteomes:UP000019183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS43 {ECO:0000313|EMBL:CDL09594.1,
RC ECO:0000313|Proteomes:UP000019183};
RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT "Antibiotic resistance diversity of beta-lactamase producers in the General
RT Hospital Vienna.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:CDL09594.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CBWK010000385; CDL09594.1; -; Genomic_DNA.
DR AlphaFoldDB; W1DN93; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR Proteomes; UP000019183; Unassembled WGS sequence.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
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; 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 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 Oxidoreductase {ECO:0000313|EMBL:CDL09594.1}.
FT DOMAIN 1..224
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 894 AA; 98917 MW; 11240385A7781E44 CRC64;
MSNLVNIYKG LCMPADLPRF YLDLADLRLE SAICLFHQRF STNTVPRWPL AQPFRYLAHN
GEINTITGNR QWARARTYKF QTPLIPDLHD AAPFVNETGS DSSSMDNMLE LLLAGGMDIV
RAMRLLVPPA WQNNPDMDPE LRSFFDFNSM HMEPWDGPAG IVMSDGRYAA CNLDRNGLRP
ARYVITKDKL ITCASEVGIW DYQPDEVVEK GRVGPGELMV IDTRAGRILH SAETDDDLKS
RHPYKEWMEK NVRRLVPFED LPDEEVGSRQ LDDDTLASYQ KQFNYSAEEL DSVLRVLGEN
GQEAVGSMGD DTPFAVLSSQ PRIIYDYFRQ QFAQVTNPPI DPLREAHVMS LATSIGREMN
VFCEAEGQAH RLSFKSPILL YSDFKQLTTM EEEHYRADVL DITFNPAEAS LSETVKALCD
KAEQMVRDGT VLLVLSDRNI AKDRLPVPAP MAVGAIQTRL VDKSLRCDAN IIVETASARD
PHHFAVLLGF GATAIYPYLA YETLAKLVDS KAIDKPYRAV MLNYRNGINK GLYKIMSKMG
ISTIASYRCS KLFEAVGLHR DVSELCFQGV VSRIGGASFD DFQQDLLNLS KRAWLARKPL
AQGGLLKYVH GGEYHAYNPD VVRTLQQAVQ SGEYSDYQQY AKLVNERPAA TLRDLLALNP
GEDAISIDEV EPAKELFKRF DTAAMSIGAL SPEAHESLAE AMNSIGGFSN SGEGGEDPAR
YGTNKVSRIK QVASGRFGVT PAYLVNADVI QIKVAQGAKP GEGGQLPGDK VTPYIAKLRY
SVPGVTLISP PPHHDIYSIE DLAQLIFDLK QVNPKAMISV KLVSEPGVGT IATGVAKAYA
DLITIAGYDG GTGASPLSSV KYAGCRGSSA WWKPSRRWLP TVCVIRSVCR WMAA
//
