ID A0A0J5FRJ2_9GAMM Unreviewed; 1485 AA.
AC A0A0J5FRJ2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KMJ44926.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KMJ44926.1};
GN Name=gltB {ECO:0000313|EMBL:KMJ44926.1};
GN ORFNames=AB204_11970 {ECO:0000313|EMBL:KMJ44926.1};
OS Xenorhabdus khoisanae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=880157 {ECO:0000313|EMBL:KMJ44926.1, ECO:0000313|Proteomes:UP000036277};
RN [1] {ECO:0000313|EMBL:KMJ44926.1, ECO:0000313|Proteomes:UP000036277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCB {ECO:0000313|EMBL:KMJ44926.1,
RC ECO:0000313|Proteomes:UP000036277};
RA Naidoo S., Featherston J., Gray V.M.;
RT "Draft Whole-Genome Sequence of the Entomopathogenic Bacterium Xenorhabdus
RT khoisanae.";
RL Submitted (JUN-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:KMJ44926.1}.
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DR EMBL; LFCV01000071; KMJ44926.1; -; Genomic_DNA.
DR RefSeq; WP_047963591.1; NZ_LFCV01000071.1.
DR STRING; 880157.AB204_11970; -.
DR PATRIC; fig|880157.4.peg.2545; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000036277; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:KMJ44926.1}.
FT DOMAIN 12..401
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1485 AA; 163149 MW; 0777C7AF38538142 CRC64;
MLYDNLQEKD NCGFGLIAHI EGEPSHKVVR TAIHALARMQ HRGAILADGK TGDGCGLLMQ
KPDRFFQMTA SEHSWRLAKN YAVGMLFLSQ DAKIAQSCRD IIEQELQNET LSIVGWREVP
INRDILGDIA LSSLPRIEQI FVNAPAGWRS QDLERRLFVA RRRIEKRITD NDFYICSLSN
LVTIYKGLCM AADLPRFYPD LADLRMESSI CLFHQRFSTN TVPRWPLAQP FRYLAHNGEI
NTITGNREWA KARAYKFRTP LIPDLHTAAP FVNETGSDSS SLDNMLELFL NGGMDLIRAM
RLLVPPAWQN NPDMDDDLRA FFDFNSMHME PWDGPAGIVI SDGRYAACNL DRNGLRPARY
VITKDKLITC ASEVGIWDYQ PDEVVEKGRV GPGELMVIDT YAGRILHSAE TDNDLKLRHP
YKEWLEKNVK RLTPFEELPE DQVGQRDLDD RLLATYHKQF AYSNEELDQI IRTLGENAQE
ATGSMGDDTP FAVLSSRPRI IYDYFRQQFA QVTNPPIDPL REAHVMSLAT RIGREMNVFC
EAEGQAHRLS FESPVLLYSD FVQLTTQQES YYRADTLDLT FNPQESSLQS AVATLCERAE
KLARNGAVLL VLSDRNISPE KLPIPAPMAV GAIQHCLVEK NLRCDANLIV ETASARDPHH
FAVLLGFGAT AVYPYLAYES LGKMVDDGTI NTPYARVMLN YRNGVNKGLY KIMSKMGIST
ISSYRCSKLF EAVGLHPEVT DVCFNGVVSR IGGADFSDFE QDLRNLSKRA WLHRHTIDQG
GLLKYVHNGE YHAYNPDVVN TLQAAVHSGK YSDYQKYSAL VNGRPVTTLR DLLAIAPKGE
LIAIEDVEPA EALFKRFDTA AMSIGALSPE AHEALAEAMN TLGGFSNSGE GGEDPARYGT
KKVSRIKQVA SGRFGVTPAY LASADVIQIK VAQGAKPGEG GQLPGDKVTP YIAKLRYSVP
GVTLISPPPH HDIYSIEDLA QLIFDLKQVN PKALISVKLV SEPGVGTIAT GVAKAYADLI
TIAGYDGGTG ASPLSSVKYA GCPWELGLVE TQQALVANGL RHKIRLQVDG GLKTGLDIIK
AAILGAESFG FGTGPMVALG CKYLRICHLN NCATGVATQD EKLRQSHYHG LPERVINYFH
FIAQETRELM AQLGVKRLID LIGRTDLLEI LEGISAKQSK LSLETLLETA EPHAGKDLHC
TEDNPPFDQG ELNKSIVTQA MPYVENAQSK TFYFDIQNTD RSVGASLSGE IAARYGDQGL
AADPIKLHFT GTAGQSFGVW NASGVELTLT GDANDYVGKG MAGGRIVILP PVGSAFKSNE
ATIIGNTCLY GATGGKLFAA GCAGERFAVR NSGAITVIEG IGDNGCEYMT GGIVCVLGNT
GVNFGAGMTG GFAYVLDESD DFRKRVNPEL VEVLSMDALA IHKEHLRGLI TEHVRLTGSQ
HGESLLENWS QWVNKFALVK PKSSDVSALL GHRSRSSAEL RVQAQ
//
