ID A0A1I1UGP9_9BACT Unreviewed; 1506 AA.
AC A0A1I1UGP9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glutamate synthase (NADPH/NADH) large chain {ECO:0000313|EMBL:SFD69907.1};
GN ORFNames=SAMN05444380_10172 {ECO:0000313|EMBL:SFD69907.1};
OS Thermophagus xiamenensis.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Thermophagus.
OX NCBI_TaxID=385682 {ECO:0000313|EMBL:SFD69907.1, ECO:0000313|Proteomes:UP000181976};
RN [1] {ECO:0000313|EMBL:SFD69907.1, ECO:0000313|Proteomes:UP000181976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19012 {ECO:0000313|EMBL:SFD69907.1,
RC ECO:0000313|Proteomes:UP000181976};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FONA01000001; SFD69907.1; -; Genomic_DNA.
DR RefSeq; WP_010527269.1; NZ_FONA01000001.1.
DR STRING; 385682.SAMN05444380_10172; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR InParanoid; A0A1I1UGP9; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000181976; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000181976}.
FT DOMAIN 21..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1506 AA; 166653 MW; C24B6B073FFF556C CRC64;
MQQRFPKVQG LYDPANEHDN CGIGFVAHIK GKPSNDIVQK GLEVLVNMTH RGAESADNKS
GDGAGILLQV PHQFFNSLSF DLPPAGSYGT GLIFLPSNPE SAKACLDILN QNIIEEGLSL
IGYRDVPVDS GVIGEIARSS EPVIRQVFVT GDFKEQDALE RKLYLLRKVT ENAVRNSNIK
GKDCFYIVSL SSKVFIYKGM LTPAQLGQYF LDLQDPRMAS AIALVHSRFS TNTFPTWDLA
QPFRILAHNG EINTIKGNRL WMQAREGLLE SDMFGEDLKK LFPIIEEGKS DSASLDNVLE
FLFLAGRSLP HALTMLIPES WNDKNPIPPS LKAYYEYHST IMEPWDGPAS IVFSDGRYIG
GTLDRNGLRP SRYVITDDDL IVMGSEVGVQ TFPADKIVAK GRLKPGKLLL VDTRLGIIIP
DEEIKAQLSR RHPYENWLKE NRISLKDIEV KHRVPSQLGE KYDVYLKTFG YNKEEIERII
SPMAQTGVEP LGSMGNDAPM AIFSEKPQRL FNYFRQLFAQ VTNPPIDPIR EGLVMALTNY
IGSVSKNLLV ENPEHCRSIK FASPIITNTD LGKIKDYRRE EFTHVTIPML FRASEGGKGL
EKALEDICRQ AEKAVDDGNN YIILSDRDVS LEYAAIPSLL ATATVHHHLI KAKKRMQVGL
IVETGEAREV MHFALLLGYG ASVINPYVCF ATINQLVEQG KIEGPYHEAR QRYIKAVDKG
ILKILSKMGI STLRSYHGAQ IFEAIGISQK VIDKCFTGTT SRIGGIGFDE IAQEALEFHQ
KAFDESLPKG PYETAGIYAY RKYGEKHAWN PETIGLLQWA TSRNDYQKYK EYSSIVEKDN
KKPLFLRGFL KFKTGNPINI DEVEPVEAIM KRFVTGAMSY GSISKEAHEA LAMAMNEIGG
RSNTGEGGED AKRFKSPARS AIKQVASARF GVTNNYLVNA DELQIKIAQG AKPGEGGQLP
GYKVDEVIAK LRHSTPGITL ISPPPHHDIY SIEDLAQLIF DLKNANPRAK VSVKLVSETG
VGTVAAGVAK AHADLIVISG TEGGTGASPT SSIKYAGLPV ELGLAEAQQT LVLNNLRGRV
KLQTDGQLKT GHDVVKMALL GAEEFGFATS SLIVLGCVMM RKCHLNTCPA GIATQDEVLR
KRFIGKYKNL VHFFTFIAME VREILAQMGY RSLDEIIGRS DLLEQDPDVK TWKTKGVDLS
ALLHFPEEGH KFPLRQTMEQ DHKIDDVLDR KLIQEARPAL QNGSRVWLAH PVNNVDRAVG
AMLSGEVSRI YGEEGLPKNT INCSFTGSAG QSFGAFLVNG VSFRLEGDAN DYLGKGLSGG
KIVVVPPTGH KFKAEENIIV GNTVLYGATS GHLYVRGMAG ERFAVRNSGA NAVVEGTGDH
CCEYMTGGRV VVIGPTGRNF AAGMSGGIAY VLDESGNFDF FCNKGLVDLM PVQDYDDIQE
LQFLLHKHLL HTNSSKAREV LVNWEKYLPK FVKVIPFEYK KVLEQQKVKE LEKKLRETED
APYLRE
//
