ID A0A1G3QDP2_9SPIR Unreviewed; 1023 AA.
AC A0A1G3QDP2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OHD64550.1};
DE Flags: Fragment;
GN ORFNames=A2176_08445 {ECO:0000313|EMBL:OHD64550.1};
OS Spirochaetes bacterium RBG_13_51_14.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802193 {ECO:0000313|EMBL:OHD64550.1, ECO:0000313|Proteomes:UP000176595};
RN [1] {ECO:0000313|EMBL:OHD64550.1, ECO:0000313|Proteomes:UP000176595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHD64550.1}.
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DR EMBL; MIBH01000044; OHD64550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3QDP2; -.
DR STRING; 1802193.A2176_08445; -.
DR Proteomes; UP000176595; Unassembled WGS sequence.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
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; 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 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;
FT DOMAIN 17..411
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 894..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1023
FT /evidence="ECO:0000313|EMBL:OHD64550.1"
SQ SEQUENCE 1023 AA; 115380 MW; ACC9430E6F63B547 CRC64;
MPQRQGLYDS SYEHDSCGIG FVAHIKGAPS YEIIMRGLEV LERMEHRGAE SADNKTGDGA
GIMMQIPHNL YKDELPSLPE PGHYGTGVVF LPRDVREAEY CIAELERVID EEGMRTLGWR
PVPVDSSVLG AISRASEPVM KQIFVGERNP QDPSTLERAL FIARKAIENR IRNSSLKEKH
LFYVPSLSSR TMVYKGMLMP NQVRHYYHDL RDQRTKSAVA LVHSRFSTNT FPSWDLAQPF
RLLAHNGEIN TIRGNRFWMS ARESSFKSDL FGDNITKILP VIEPDKSDSA SFDNALEMLS
FTGRSLPHAL MMLIPESWNE KNPIPEELKY FYEYHSTFME PWDGPASMVF CDGRYVGGTL
DRNGLRPSRY VITHDDLIVM ASEVGVQTFP AEKIAYKGRL MPGKLLLVDM EQGRIIPDEE
IKRRIYTQKP YRLWVQLNRV NLEDLEIQGD VPVAIDEDRL HEMHLLYGYT REDLEDIITP
MVETAQEPTG SMGTDTPLAV FSDKPQRLFN YFKQCFAQVT NPAIDPIREE LVMTLTSYIG
EQKNLLNETP EHCRMIKLKS PIFTNREVEN IRKNEKTESK TITLPMTFPV KTAPGSMKRA
LDALCVAVED KIDSGYRYII LSDREADKDN APIPSLLACA GVHHHLIRTK KRTLIGLIIE
TAESREVMHF ALLFGYGASA VNPYGAFATI HSMVNRGELG NTSYLKAEDY FIKAVNKGLL
KVLSKMGTST LRSYRGSQIF EAIGLGKELI DTCFTGTESR IGGIGFAEAE REALMQHDIA
YKKRPKLLES PGVYQYRNRG ERHAWNPESI YLLQWATRTG DYGIYKEFSR FMNEQTRTPH
FIRGLFDFKP QKPISIDEVE PEKNILKRLV TGAMSFGSIS KDAHETIAAA MNRLQGRSNS
GEGGEDPERF EKRPDGTWTR SAIKQVASGR FGVTSNYLAN ADELQIKIAQ GAKPGEGGQL
PGHKVDTIIA KTRHSTPGVT LISPPPHHDI YSIEDLAQLI FDLKNANPKA RISVKLVSET
GVG
//