ID A0A1G1NI34_9BACT Unreviewed; 1503 AA.
AC A0A1G1NI34;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OGX29332.1};
GN ORFNames=A3B78_01450 {ECO:0000313|EMBL:OGX29332.1};
OS Omnitrophica WOR_2 bacterium RIFCSPHIGHO2_02_FULL_67_20.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801860 {ECO:0000313|EMBL:OGX29332.1, ECO:0000313|Proteomes:UP000180285};
RN [1] {ECO:0000313|EMBL:OGX29332.1, ECO:0000313|Proteomes:UP000180285}
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 -!- 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:OGX29332.1}.
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DR EMBL; MHGT01000012; OGX29332.1; -; Genomic_DNA.
DR STRING; 1801860.A3B78_01450; -.
DR Proteomes; UP000180285; 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 26..423
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 908..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1503 AA; 163570 MW; 2FF4DCC528840178 CRC64;
MLPSVRTSGF PQPEGLYDPA YEHDACGTGF VASIDGIASH AIVRSAIQCV CNVTHRGAVS
ADAKTGDGAG ILTQIPQPLF AKALKQLKAA PAAVGDLAVG VIFLPQDERA RTAAQRQVER
TVSTCALTLI GWREVPVDPS VLGEEALETQ PVIRHLLVRR PASAPAAEFE RRLFLARRRI
EHGWARERLS GCYIPSFSSR TIVYKGLLVA PQLAHFYRDL SDADYASAIA VFHQRYSTNT
FPNWFLAQPF RFLGHNGEIN TLQGNRNWMA AREAELSSTR WGKELRELFP IVQPGGSDSM
SLDNVLELFV MSGRDILQSM MMLVPDAWQG MRDIDIDPQV RAFYQYHATL MEPWDGPAAL
TFTDGVIVGA TLDRNGLRPA RYWVTRDRTV IMASEVGVVE VDPARIVEKG RLGPGHVFAV
DTRRKRLLRN EEIKREYAAV APYAEWVEQS TVPLSQIVNG HIADEVNVEP ASLTRHQLAF
GITEEEVQMV IEPMAKTGKE PIWSMGDDVP LSVLSAKPKP LFTYFKQLFA QVTNPPIDPI
REELVMSLNT LLGARPNPLS TGPAPKRMLR AGSPLLFPQE LAALRSLRQR DLKSATLSTL
FETAGGPAAL RSAVKRLREQ AVKAVDAGAT ILILSDHELD QTHAPIPSLL ATAAVHHHLI
RTGRRMKASL VVETGEAHEV HQVACLIGYG AAAVYPYLAY QTIKALASAG RLGDDTFEQA
LARFRKAVDQ GVLKIMSKMG ISTVGSYRGA QIFEALGIAK ELIDECFPGT PSRIGGVTYE
HIAAEVLAWH RRAYQTQGPL HLDAGGFYKY RRDGEYHAFN PEMVRYLQQS IKVGDFDSYK
KFAASVNTRP PMVLRDLLEV KPLGPAVPLE EVEPIEAITR RFATASISYG ALSLEAHETL
AIAMNRIGGK SGSGEGGEDP SRYHPTDPKM NRSSAIKQVA SGRFGVTPEY LMSASELEIK
MAQGSKPGEG GQLPGHKVSD DIARVRHTIP GISLISPPPH HDIYSIEDLK QLIYDLKMIN
PAARVNVKLV SEAGVGTIAA GVAKGYADTV LISGHDGGTG ASPLSSIKNA GLPWELGLAE
TQQTLRLNGL RERILVRTDG GMKTGRDVLL AAVFGAEEYG FGTAAVVATG CVMTRQCHLN
TCPVGVATQD PKLRARFAGT PEMVMNYFIF VAQELREYMA SLGARRLEEL IGRTDLLVRR
EVQLHEKAAT VNLDYLTATV DAGPRVHTVA RNNEPGQPLD ERLVKDAAAA LEGGAKVKLS
YPIRNIHRTV GARLAGEIAK RYGDKGLPPA SVDVLLTGVA GQSFGAFCIN GMRLTLVGEA
NDYVGKGMAG GELIIRPPDE SPFAWHKNTI IGNTCLYGAT GGVLYAAGRA GERFAVRNSG
GMAVVEGLGD HGCEYMTGGI VLVLGETGRN FGAGMTGGRA YVLDRERVFE KRVNLELVEL
HRLEGQEDVD NVRALLERHF VSTKSNLALE ILTNWDDTQE LFWMVVPRGA GAKLELAVSA
KEG
//
