ID A0A089ID57_9BACL Unreviewed; 1531 AA.
AC A0A089ID57;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:AIQ22261.1};
GN ORFNames=H70737_05000 {ECO:0000313|EMBL:AIQ22261.1};
OS Paenibacillus sp. FSL H7-0737.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ22261.1, ECO:0000313|Proteomes:UP000029519};
RN [1] {ECO:0000313|EMBL:AIQ22261.1, ECO:0000313|Proteomes:UP000029519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ22261.1,
RC ECO:0000313|Proteomes:UP000029519};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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}.
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DR EMBL; CP009279; AIQ22261.1; -; Genomic_DNA.
DR RefSeq; WP_042185239.1; NZ_CP009279.1.
DR KEGG; paej:H70737_05000; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR HOGENOM; CLU_000422_8_2_9; -.
DR Proteomes; UP000029519; 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 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:UP000029519}.
FT DOMAIN 22..421
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 911..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1531 AA; 168311 MW; 95448531B0753E70 CRC64;
MRHTELPGKQ GLYDPQFEKD ACGMGFVAHI KGKPSHDIVS NALTMLFNME HRGGQGSEPN
SGDGAGIMLQ IPHRFFVSEA QKLGFALPEQ GHYGVGMIFL SHNEKVRAQH EALLSKIIAE
EGQEVLGYRD VPTYDEMLGK TAKAAKPFVR QVFIGRSASV TNELSFERKL YVIRKRAELA
IRYGGVEEAE AFYIPSLSCR KIVYKGMLTT EQVGQFYLDL QNEELESAIA LVHSRFSTNT
FPSWERAHPY RFMIHNGEIN TLRGNVNWMH ARQSLFKSEV FGEDLSKIKP VINPDGSDTA
MFDNTFEFLY LSGRSLTQVA MMMVPEPWSN HDSMDADKKA FYEYHSTLME PWDGPAAMGF
TDGVQIGAIL DRNGLRPARY YVTKDDMIIL SSEAGVLDIP AEDILYKDRL KPGRMLLVDT
KEGRIISDEE VKSAIATEKP YRQWLDEHLI SLEELPDAPE LPNPKHDNVQ QLQQAFGYTF
EDLRKVLEPM ASTGAEAVGS MGYDAPLAVL SDRPQRLYNY FKQMFAQVTN PPIDAIREEL
VTSTTTTIGP ERNLLKPEPE SCRQISLHTP ILSNEDFAKI RHVRRAGFKS MSIPILFPAE
LGAEGMRIAL ERMNEAADRV MAKGHNILIL TDRGVDRENA AIPALLAVSS LHHHLIRQGT
RTKVSILLES GEPREVHHYA LLLGYGVSAV NPYLAFESLD DMIGQGLLRG ISHEKAVKNY
IKAATKSVVK ILSKMGISTI QSYRGAQIFE AVGLNSEFVD RYFTWTPSRI GGIGLEEVAT
EALIHHNRAF TEKDGNDKVL DSGGDYQWRN DGEDHLFNPQ TIHLLQHSVR SGDYKLYKKY
AALVQGESEK HLTIRSLLQF KSAYEPISLE EVEPVESIMK RFKTGAMSFG SISKEAHETL
AIAMNRIGGK SNTGEGGEDP ARYIPDSNGD SRRSAIKQVA SGRFGVTSNY LVNADEIQIK
MAQGAKPGEG GQLPGRKVYP WVAEVRGSTA GVGLISPPPH HDIYSIEDLA ELIYDLKNAN
PRANINVKLV SEVGVGTIAA GVAKGRADII LVSGYDGGTG ASPMNSIRHA GLPWELGLAE
THQTLMLNNL RDRVVLETDG KMLSGRDLAV AVLLGAEEYG FATAPLVAVG CIMMRVCQMD
TCPVGVATQN PDLRKNFTGD PQHVVNFMTF VAQDLREIMA SLGFRTIEEM VGRTDCLDAA
QASQHWKKKG VDLSSLLHVP EMPEGSTRFC SKRQNHGLEE TLDVSKLLDL AAPALESGTA
VEASLPITNV NRAVGTILGS ELTRKYGAAG LPDDTIRLHF TGSAGQSLGA FVPKGITLTV
EGDSNDYVGK GLSGGKIIIK PSPKATFAAE DNIIIGNTAF YGATAGEAYI NGIAGERFAV
RNSGAKVVVE GVGDHGCEYM TGGRVVVLGE TGRNFAAGMS GGIAYVYDPE RSFIGRCNLE
MVLLERVEEP EEIEELRELI SRHVELTGSK AGARVLDQWA DSLPKFVRVI PKDYKRMMEQ
IRKVEQTGLT GEAALMAAFE ANMRELARVG G
//
