ID A0A089JY31_9BACL Unreviewed; 1531 AA.
AC A0A089JY31;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:AIQ39523.1};
GN ORFNames=R50912_05340 {ECO:0000313|EMBL:AIQ39523.1};
OS Paenibacillus sp. FSL R5-0912.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536771 {ECO:0000313|EMBL:AIQ39523.1, ECO:0000313|Proteomes:UP000029512};
RN [1] {ECO:0000313|EMBL:AIQ39523.1, ECO:0000313|Proteomes:UP000029512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0912 {ECO:0000313|EMBL:AIQ39523.1,
RC ECO:0000313|Proteomes:UP000029512};
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; CP009282; AIQ39523.1; -; Genomic_DNA.
DR RefSeq; WP_042241606.1; NZ_CP009282.1.
DR KEGG; paeq:R50912_05340; -.
DR HOGENOM; CLU_000422_8_2_9; -.
DR Proteomes; UP000029512; 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:UP000029512}.
FT DOMAIN 22..421
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1531 AA; 167821 MW; 5F2ABD6E6284F2AE CRC64;
MRHTELPGKQ GLYDPQFEKD ACGMGFVAHI KGKPSHDIVS NALTMLFNME HRGGQGSEPN
SGDGAGIMLQ IPHRFFAGEA AKLGFELPEQ GHYGVGMIFL SHNEEIRARH EALLSEIIAE
EGQQVLGYRD VPTFDEMLGK TAKAAKPYVR QVFIGRSEGI KDDLSFERKL YVIRKRAELS
IRYGGAEEGE SFYVPSLSCK KIVYKGMLTT VQVGQFYLDL QDEKLESAIA LVHSRFSTNT
FPSWERAHPY RFMIHNGEIN TLRGNVNWMH ARQSLFKSEV FGEDLGKIKP VVNPDGSDTA
MFDNTFEFLY LSGRSLPHVA MMMVPEPWSN HDSMDGKKKA FYEFHSTLME PWDGPAAMGF
TDGVQIGAIL DRNGLRPARY YVTKDDLIIL SSEAGVLDIP AEDVLYKDRL RPGRMLLVDT
KQGRIISDEE VKAEIAAEQP YQDWLDEHLI SLDELPEAPE LPNPKHDNVQ QLQQSFGYTF
EDLRKVLEPM ASTGAEAVGS MGYDSPLAVL SDRPQRLYNY FKQMFAQVTN PPIDAIREEL
VTSTATTIGP ERNLLKAEPE SCRQISLDSP ILSNEDFAKL RHVRRAGFKS MSIPILFPAE
LGAEGLRIAL ERMNEAADRV MAKGHNILIL SDRGVDRDNA AIPALLAVSS LHHHLIRSGT
RTKVSILLES GEPREVHHYA LLLGYGVSAV NPYLAFESLD DMIGQGLLRG ISHEKAVKNY
IKAATKSVVK ILSKMGISTI QSYRGAQIFE AVGLNSEFVD RYFTWTPSRI GGIGLEEVAL
EALASHNRAF TDKDGNDKVL DSGGEYQWRS DGEEHLFNPQ TIHLLQHSVR SGDYEMYKKY
AALVQGESEK HQTLRSMLQF KPANGPVPLD EVEPAESIMK RFKTGAMSFG SISKEAHETL
AIAMNRIGGK SNTGEGGEDP ARFIPDANGD SRRSAIKQVA SGRFGVTSNY LVNADEIQIK
MAQGAKPGEG GQLPGRKVYP WVAEVRGSTA GVGLISPPPH HDIYSIEDLA ELIYDLKNAN
PRANINVKLV SEVGVGTIAA GVAKGRADII LISGYDGGTG ASPMNSIRHA GLPWELGLAE
THQTLMLNNL RDRVVLETDG KMLSGRDLAV AVLLGAEEYG FATAPLVAVG CIMMRVCQMD
TCPVGVATQN PELRKNFMGD PQHVVNFMTF VAQDLREIMA ELGFRTIEEM VGRTDCLDAV
QASTHWKKQG VDLSSLLHTP AMPEGSTRFR SKHQNHGLEE TLDMTHLLDI AAPALESGTA
VEASLPITNV NRAVGTILGS ELTRKYGAAG LPDDTIKLYF TGSAGQSLGA FVPKGITITV
EGDSNDYVGK GLSGGKLIIR PSRKATFAAE DNIIIGNTAL YGATGGEAYV SGIAGERFAV
RNSGANVVVE GVGDHGCEYM TGGRVVVLGE TGRNFAAGMS GGIAYVYDPD STFIKRCNLE
MVLLERVEEA DEIAELHGLI TRHTELTDSN AGRTILDSWD QALPKFARVI PKDYKRMMEQ
IRKVEQNGLT GEAALMAAFE ANMRELARVG G
//
