ID A0A1U7DWB7_9FLAO Unreviewed; 1503 AA.
AC A0A1U7DWB7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:APY12774.1};
GN ORFNames=BWZ22_05795 {ECO:0000313|EMBL:APY12774.1};
OS Seonamhaeicola sp. S2-3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1936081 {ECO:0000313|EMBL:APY12774.1, ECO:0000313|Proteomes:UP000187101};
RN [1] {ECO:0000313|EMBL:APY12774.1, ECO:0000313|Proteomes:UP000187101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2-3 {ECO:0000313|EMBL:APY12774.1,
RC ECO:0000313|Proteomes:UP000187101};
RA Chi W.-J., Kim J.H.;
RT "Complete genome sequence of Seonamhaeicola sp. S2-3 isolated from seawater
RT in Jeju island.";
RL Submitted (JAN-2017) 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; CP019389; APY12774.1; -; Genomic_DNA.
DR STRING; 1936081.BWZ22_05795; -.
DR KEGG; seon:BWZ22_05795; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000187101; Chromosome.
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:UP000187101}.
FT DOMAIN 16..411
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 897..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1503 AA; 167919 MW; 79AC14930CCE568D CRC64;
MQKQGMYSPD YEHANCGAGF ICNLKGEKTN QIIHDALEIL VKLEHRGGVS ADGKTGDGAG
LLIDIPHDYF KRVCEFEIPA PREYAVGMVF LPKVANQYQY CKDVFEREVK AQGLTILGWR
KVPVDSSQLG EIAKASEPNI EQLFISKPEG ATEANFKAKL YAARKITEHD IRLSKISQSD
YFYVPSLSTT TLIYKGIIMP EDIGPYYTDL QQKDLVTRLA LVHQRFSTNT MPTWELAQPF
RFMCQNGEIN TLRGNVSRMR IREEIMKSDV FGPQIDKLFP IVLPGKSDSA SMDMVVELLT
HTDRSLPEIM MMMIPEAWEK HKTMSEDKKA FYEYNCCIME PWDGPASIPF TDGDYIGALL
DRNGLRPSRY TLTKSGKLIM SSEVGVVDVD PADVELHGRL EPGKMFLVDM NEGRIIDDEE
IKNKIVSERP YKEWLDKTRL HLRDVPYTNE TCPIETIDIK TRQRLFNYTI EDIQEVITPM
AQKGKEALGS MGTDTPLAVL SDRPQLISNY FKQLFAQVTN PPLDGIREEI VTDISLNLGK
DRNIFSITER QCRKLRIQNP VISNADLEKI RTIKIEGFKA ETIHMLYPKA QGMNGLEDAL
EDIIKQVEKA LERKTNIIIL SDRGVNKDFA PIPALLACSY VNHQLNRLRK RSYFDIIIES
AEPREPHHFA TLFGYGASAI NPYMVNEIIR DQVKEGFIKG IDEQKAVDNF NKAIGKGILK
IMNKIGISTL HSYRGSQIFE IVGFNSSFVE KYFPYTTSRI EGIGLYEIEK EINERYKYAY
PDKEIKNRLG LNIGGDYRWR RNGERHMFNP TTVAKLQQAV RLSDQKSYDI YAKAINEQSE
NLMTIRGLFE FDNLDPIPIE EVEPWTEIVK RFKTGAMSYG SISREAHENL AIAMNRIGGK
SNSGEGGEDR RRFQKDINGD SRNSAIKQVA SGRFGVTSHY LTNAKEIQIK MAQGAKPGEG
GQLPGEKVLP WIADARNSTP FVGLISPPPH HDIYSIEDLA QLIFDLKNAN RDARINVKLV
SEVGVGTIAA GVSKAKADVV LISGYDGGTG ASPLTSLKHA GLPWELGLAE AQQTLVLNNL
RSRIVVECDG QLKTGRDVAI AALLGAEEFG FATAPLVASG CIMMRKCHLN TCPVGIATQD
KELRKNFKGT PEHVINFFYY VAEELRGIMA QLGFRTLAEM VGQTHKINAT KAIKHYKAKG
LDLSNILHRP AEYNKLTIRN TEKQDHDLDN VLDFTILQDS HRALYRKEKT NLAYPIKNIN
RTVGAIVSNE ISKIYGHLGL PEDTLNIKFT GSAGQSFGAF GAHGLTFTLE GNANDYLGKG
LSGAKLIVKK PAEADFVAEE NIIVGNVCLF GAVQGEAYIN GIAGERFAVR NSGATAVVEG
VGDHCCEYMT GGKIVVLGKT GRNFAAGMSG GYAFVLNESG QFTNGLCNEE TIDFDPITEA
DEAELKQLIT NHVAYTNSDK GKEILAHWNN YLPKFVKVMP KEYKVALERI ANEEPMVEEL
TIA
//
