ID A0A0Q6BNJ2_9PROT Unreviewed; 1556 AA.
AC A0A0Q6BNJ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KQT42602.1};
GN ORFNames=ASG34_07700 {ECO:0000313|EMBL:KQT42602.1};
OS Methylophilus sp. Leaf416.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylophilus.
OX NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT42602.1, ECO:0000313|Proteomes:UP000050891};
RN [1] {ECO:0000313|EMBL:KQT42602.1, ECO:0000313|Proteomes:UP000050891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT42602.1,
RC ECO:0000313|Proteomes:UP000050891};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT42602.1, ECO:0000313|Proteomes:UP000050891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT42602.1,
RC ECO:0000313|Proteomes:UP000050891};
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:KQT42602.1}.
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DR EMBL; LMQS01000002; KQT42602.1; -; Genomic_DNA.
DR RefSeq; WP_055828897.1; NZ_LMQS01000002.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000050891; 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 41..438
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1556 AA; 169101 MW; 69A1BF34F3C243FC CRC64;
MQPDNNLMSA SQDSATALDS QLGLAPQSQG LYDRRHEKDS CGVGFVAHIK GQKSHDIVAK
GLQLLDNLTH RGATGYDPKL GDGAGLLMQM PDTFMREEAT KLGMTLPVAG QYAVGQAFLP
QNAENRAKCE AIFAQIIAEE NQTLLGWRDV PVDNSNIADA ARAVEPVMRQ VFIASTVSDN
NAFERKCFVI RKRIEHAIRA LALQDNAQFY MPSFSSRTIV YKGMLLANEV GVYYKDLKDA
RVVSALALVH QRFSTNTFPA WDLAHPFRMI AHNGEINTVQ GNVNWMTARH ETIKSVVLGE
DLEKLWPLIV EGQSDSACFD NCLELLVAGG YSLPHAMMML IPEAWNNNPL MDEDRRAFYE
YHANIMEPWD GPAAVAFTDG KMIGATLDRN GLRPARYLVT EDDIVMMASE MGVITFPQEK
IVKKWRLQPG KMLLIDMEQG RIIDDEEVKK ELAQAKPYRQ WIEQTRFHVT ELPNVGSGEV
TLQASLLDTQ QAFGYSQEDL KFVLQPMLDN GEEGAGSMGN DAALPVLSNK AKTLYNYFKQ
LFAQVTNPPI DPIREELVMS LVTFIGPKPN LLAVDETNPP LRLEGSQPVL SLDGLEILKQ
IDTLTKGQFK SIVLDLTYDA SLGKNGMKQA LDTLHDQAEK AVHDGYNILI LSDRTVSATR
VAIPALLACS ATHEFLVKAG LRTSTGLVID TGSAREVHHF ALLAGYGAEA VCPWLVYETM
KTMTGDAEKA GKNFMKAIGK GLYKVMSKMG ISTYQSYCGA QIFEAIGLNS QFVNDYFTGT
VSQIEGIGLE QVAEETMRMH DQAFGNDPTL SNSLEAGGEY AFRVRGEEHL WTPQSISKLQ
SATRTGQYDT YKEYAALIND QSRRHMTLRG LFEIKPAAAA IPLEQVESAK EIVKRFATGA
MSLGSISTEA HATLAVAMNR IGGKSNTGEG GEDVKRFIPV QIDSSIAKVL GSELIEADVP
LKAGDSMRSR IKQVASGRFG VTAEYLSSAD QIQIKMAQGA KPGEGGQLPG HKVSPYIAKL
RFSVPGVGLI SPPPHHDIYS IEDLAQLIHD LKNANPQASI SVKLVSETGI GTVAAGVAKA
KSDHIVVAGH DGGTGASPLS SVKHAGTPWE LGLAETQQTL VLNQLRGRVV LQVDGQMKTG
RDVLIGALLG ADEFGFATAP LVVEGCIMMR KCHLNTCPVG VATQDPELRK KFTGQPEHVV
NYFFFVAEEL RELMASIGIA KFEDLIGRAD LLDMKAGIEH WKINGLDFSK IFHLPDMPAS
VSRKNNDIQD HGIAKALDNQ LIALSQAALE KGEKVILDLP IMNTNRTAGT MLSHEVARRY
GNDGLPHDTI HVNFTGTSGQ SFAAFLAKGI TFELTGEGND YVGKGLCGGR IIIKPPTTFR
GLSYENIIVG NTVMYGATTG ESFLSGVAGE RFGVRNSGAT AVIEGVGNHG CEYMTGGTVV
VLGQTGQNFA AGMSGGIAYI YDVDGQFSKR CNMSMVSLEK VEAAEADVGK VQHLGQPDEV
ILKGLIEQHA ALTGSPRAKD ILADWPAERA KFVKVFPNEY KRVLTEMAAA SAKQAA
//
