ID A0A0Q9ZXT0_9GAMM Unreviewed; 1489 AA.
AC A0A0Q9ZXT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KRG37709.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KRG37709.1};
GN Name=gltB {ECO:0000313|EMBL:KRG37709.1};
GN ORFNames=ARC20_02120 {ECO:0000313|EMBL:KRG37709.1};
OS Stenotrophomonas panacihumi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=676599 {ECO:0000313|EMBL:KRG37709.1, ECO:0000313|Proteomes:UP000051802};
RN [1] {ECO:0000313|EMBL:KRG37709.1, ECO:0000313|Proteomes:UP000051802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16536 {ECO:0000313|EMBL:KRG37709.1,
RC ECO:0000313|Proteomes:UP000051802};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (OCT-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:KRG37709.1}.
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; LLXU01000131; KRG37709.1; -; Genomic_DNA.
DR RefSeq; WP_057649219.1; NZ_PZOY01000002.1.
DR STRING; 676599.ARC20_02120; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000051802; 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:KRG37709.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051802}.
FT DOMAIN 24..413
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 897..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1489 AA; 162991 MW; 87D37C9BC31EDEF2 CRC64;
MAPRTRQGLE QPGLYDARDE RDACGFGMIA QLDDQPSRAL VDTAIAALSR MTHRGGVAAD
GLTGDGCGLL IRKPDPFLRA LARDAGIAIG ARYAAGVVFL PHDDAEAARC RQALEAELQR
AGTLPRGWRL VPTDDSVCGQ LARDTLPRIE QVFVDAAAGQ DDDAFALALF LARRRAEQSL
REVADFYVTT LTPNAISYKG MVLPDKLSTF YPDLQRSDLS SSAIVFHQRF STNTLPRWPL
AHPFRMLAHN GEINTIEGNR RWAQARSKVW KTPRFDIAEF NPVISMKGSD SQSLDNMLEL
LIAGGMDLLQ ALRILVPPAT QSLEFKDADL AAFYEFHGLN TEPWDGPAGI VACDGRYAAA
MLDRNGLRPA RWMLTSDRHF LVASEAGVWE LPAERITRKG KLGPGEMMAI DLKRGDLLDS
DAIDRINRAR APYKQWLHQG VTYLQTELID PSLVEEPFSE QTLRSYHKLF QLSTEEVEQV
LRPLAETEQE ATGSMGDDTP MAVLSQHTRP LYDYFRQAFA QVTNPPIDPL RESCVMSLTT
QLGKETNVFH AGPETVNHVI LNSPVLSQRK LRQLLKMPQY VERNRLIDLS YSVEEGLKAG
IERICRETEQ AAREGVVMLL LSDRYPVADR PMVHALMATG AVHHHLSALG LRCDVNLIIE
TGTARDPHHM ACLLGFGATA VYPYLAYQTL FDLGRRGILE LKKGGEQSQI GRSYRKGVYK
GLSKIISKMG ICTIASYRGA QLFEIVGLDP EVVELCFPET ASRIGGVDLA RLDHEARDLT
ARAWNDLLKP EVGGLLKYVH GGEYHMYNPD VVLTLQRATR TGDAADWQRY MDAVHSRPPS
ALRDLLQLKR ADAPTPLDEV APAEDVLRRF DTAAISLGAL SPEAHEALAI AMNRLGGRSN
SGEGGEDPAR YGTEKRSKIK QVASGRFGVT PEYLVNAEVL QIKVAQGAKP GEGGQLPGHK
VNELIARLRY AKPGIGLISP PPHHDIYSIE DLAQLIYDLK QVNPEALVSV KLVSHAGVGT
IAAGVVKAGA DLITVSGHDG GTGASPVSSI RYAGVPWELG VAESHQALVG NDLRARTLLQ
TDGGLKTGLD VVKAALLGAD SFGFGTAPMI VLGCKYLRIC HLNNCATGVA TQDERLRANY
FTGLPERVEN FFRLLAEEVR QWLSYLGVRS LDEIVGRTDL LQQLEVSPRE GVRVDLSRLL
KPAHFEGSHC AAQRLYESPD SLATQMDGLL AKAIAEKTGG DHRFLIHNTD RSIGARLSGA
IARVHGNHGM EDAPLNLRFR GTAGQSFGAF NAGGLNLELE GEANDYVGKG MAGGRVVIRP
PRGARFEARS TPILGNTCLY GATGGELFAA GRAGERFGVR NSGALAVIEG AGDHCCEYMT
DGVVLVLGKV GLNFGAGFTG GLAYVLDIER DFVDRYNHEL IDIHRISAEG FENHRQHLHK
LISRHRELTG SIWAQQILDE FRDYVGKFWL VKPKAASIES LTESLRRAA
//
