ID A0A0Q9JPU4_9BACL Unreviewed; 1534 AA.
AC A0A0Q9JPU4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KRE29803.1};
GN ORFNames=ASG81_26290 {ECO:0000313|EMBL:KRE29803.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE29803.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE29803.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE29803.1,
RC ECO:0000313|Proteomes:UP000051180};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRE29803.1}.
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DR EMBL; LMRV01000088; KRE29803.1; -; Genomic_DNA.
DR RefSeq; WP_056641570.1; NZ_LMRV01000088.1.
DR STRING; 1736388.ASG81_26290; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000051180; Unassembled WGS sequence.
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}.
FT DOMAIN 24..423
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 910..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1534 AA; 169056 MW; 59645C6806E41966 CRC64;
MKEHILGLPP KQGLYDPQFE KDACGMGFVA NIKGIKSHKV IRQALMLLEN MEHRGGQGSE
PNTGDGAGIL LQIPHAFFAA ELMKQEIKLP AEGHYAVGMI FMPQDEAARI AIEREVEAIV
QEENQSVIGW RTVPTNDKKL GESALAVKPF VRQLFIGMND SLKDNMAFER KLYVIRKRAE
LAIRYAGKEG GNMFYFSSLS SRKIVYKGML TTEQVRSFYT ELNDESVVSA MALVHSRFST
NTFPSWERAH PFHYMIHNGE INTLRGNVNW MHARQTLFAT ELFGDDIEKI KPVINPDGSD
TAMFDNTLEF LFLSGRSMAH AAMMMVPEPW SNHEKMSDER KAFYEYHSTL MEPWDGPAAL
GFTDGVKIGA VLDRNGLRPA RYYVTKDDHI ILGSEAGTVA IPPEDILYKD RLRPGRMLLV
DTEKGRIISD EEVKAEIETE HPYREWLNEH LVDLEDLPDA PELPEPNHAT VQMRQQAFGY
TFEDVRKVLE PMAGSGAEPI ASMGYDAPLA VLSERPQRLY NYFKQLFAQV TNPPIDAIRE
EIITSTGTTI GPERNLLNPE PESCRHIKLD TPILSNEQFA KLRHVRRPGF RSITLPIFFP
ANEGESGLRA ALAQMCEAAD RVIAKGHNLL ILSDRGVDKD NAAIPALLAV SALHHHLIRQ
GTRTKVAILL ESGEPREVHH FALLLGYGVS AVNPYLAFET LDDMIRQGML RGISHDKAVK
NFIKAATKGV VKILSKMGIS TIQSYRGAQI FEALGLKEEV INEYFTWTPS RIGGIGLDVI
AEETLKHHSR AFAEQEGGEK ELDSGGEYQW RKDGEDHLFT PQTIHTLQMA SRANDYKLYK
KFSALVQGED KKHLTLRSLL QFKEGRQSVP LEEVESIESI VKRFKTGAMS FGSISKEAHE
SLAIAMNRLG GKSNTGEGGE DPARFIPDAN GDSRRSAIKQ VASGRFGVTS NYLVNADEIQ
IKMAQGAKPG EGGQLPGLKV YPWVAEVRGS TPGVGLISPP PHHDIYSIED LAELVHDLKN
ANPRARINVK LVSGVGVGTI ATGVAKGRAD VIMVSGYDGG TGASPMGSIR HAGLPWELGL
AETHQTLMLN KLRDRVVLET DGKMMNGRDV AVAVLLGAEE YGFSTAPLIV LGCIMMRVCQ
LDTCPVGVAT QNPDLRKKFM GDPSHVVNYL RFIAEELREI MAELGFRTIQ EMIGRVDILE
TKQLREHYKV KGIDLSGLLY EADLPHDAVR YNVQEQNHGL ELSLDMQQLV PLAQAALENG
ERVRGTFPIL NTNRVVGTIL GSEVTRRYGA AGLPEDTISY HFVGTAGQSF GAFVPNGITL
SIEGDSNDYV GKGLSGGKII VAPSPKATFV AEDNVIIGNT ALYGATSGQA YIRGTAGERF
AVRNSGANVV VEGVGDHGCE YMTGGRVVIL GNTGRNFAAG MSGGVAYIYD EKGDFYNHCN
LEMVLLERLE DSLDIAELRG LIESHAQYTE SAIATLILND WDVSLSKFVK VIPKDYKRML
EQIRKVEDSG LVGDAALLAA FEANKKELAR AGGK
//
