ID A0A1B9XWI2_9FLAO Unreviewed; 1503 AA.
AC A0A1B9XWI2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OCK41910.1};
GN ORFNames=BA195_13080 {ECO:0000313|EMBL:OCK41910.1};
OS Tenacibaculum soleae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=447689 {ECO:0000313|EMBL:OCK41910.1, ECO:0000313|Proteomes:UP000093186};
RN [1] {ECO:0000313|EMBL:OCK41910.1, ECO:0000313|Proteomes:UP000093186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-KL19 {ECO:0000313|EMBL:OCK41910.1,
RC ECO:0000313|Proteomes:UP000093186};
RA Eisen J.A., Coil D.A., Lujan K.M.;
RT "Draft Genome Sequence of Tenacibaculum soleae UCD-KL19.";
RL Submitted (JUN-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}.
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:OCK41910.1}.
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DR EMBL; MAKX01000041; OCK41910.1; -; Genomic_DNA.
DR RefSeq; WP_068706301.1; NZ_MAKX01000041.1.
DR STRING; 447689.BA195_13080; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000093186; 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:UP000093186}.
FT DOMAIN 16..411
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 897..922
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; 167513 MW; 60704700AAD11DEE CRC64;
MEKQGLYLPE FEHENCGAGF ICNLNGERTN KIIHDALEIL VKLAHRGGVS SDGKTGDGAG
LLIDIPHNYF KRVCDFTIPN QREYAVGMVF LPKNINQYNF CKTTFEKEVV SQGLTVLGWR
KVPVDASQLG EIAFKLEPNI EQLFINKPEK ISETTFKAKL YAARKIAEHT IRKSKTSESA
YFYVSSLSIT TIIYKGIIKP EDIGAYYKDL QEQDLVTRLA LVHQRFSTNT MPTWELAQPF
RYLCQNGEIN TLRGNISRMR VREEIMKSDV FGSQIDKLFP IILPGKSDSA SMDMVVELLT
HTDRSLPEIM MMMIPEAWEK HKTMSKERKA FYEYNSCIME PWDGPASVPF TDGDYIGALL
DRNGLRPSRY TVTKSGNLIM SSEIGVVDVA PEDVKEHGRL EPGKMFLVDM NEGRIIEDEE
IKSKIVSERP YQEWLNKTRL HLKDVPYTGK TCPIESVDIK TRQRLFNYTF EDIQEVITPM
AIVGKEALGS MGIDTPLAVL SDQPQLISSY FKQLFAQVTN PPLDGIREEI VTDISLNLGK
DRNIFSITER QCRKLEIQNP VISNDDLEKI RNISVESFKA ETIEILYKKS EGLNGLEDAL
ESIVVQVEKA LTRKTNIIIL SDRGVNKEFA PIPALLACSF VNHQLNRLRK RSFFDIIIES
AEPREPHHFA TLFGYGASAI NPYMVNEIIR SQVKEGFITG MDEQKAVDNF NTAIGKGILK
VMNKIGISTL HSYRGSQIFE IVGFNSQFVE KYFPYTASRI EGIGLYEIEK EIDKRYKQAY
PSKEIDKNLS LNIGGNYRWR RNGERHLFNP TTVAKLQQAV RLSDQDSYNV YAKAINEQSE
SLMTIRGLFE FNNLDPIPLD EVEPWTEIVK RFKTGAMSYG SISREAHENL AIAMNRIGGK
SNSGEGGEDR KRFQKDVNGD SRNSAIKQVA SGRFGVTSHY LSSAKEIQIK MAQGAKPGEG
GQLPGEKVLP WIASARNSTP FVGLISPPPH HDIYSIEDLA QLIYDLKNAN REARINVKLV
SEVGIGTIAA GVAKAKADVV LISGYDGGTG ASPLTSLKHA GLPWELGLAE AQQTLVLNKL
RSRIVVECDG QLKTGRDVAI AALLGAEEFG FATAPLVASG CIMMRKCHLN TCPVGIATQD
KELRKNFKGT PEHVINFFYY IAEELRQIMA QLGFRTLAEM VGQTDKINAN KAIKHYKAKG
LDLSSILHRP EAYKSMSLKN TENQEHNLEN VLDFTILKDS HRALYRKEKM NLTYSIKNTN
RTVGAIVSHE VSKIYGHLGL PEDTLNLNFT GSAGQSFGAF GAHGLTFTVD GNTNDYLGKG
LSGAKLIVKK PDKADFIAEN NIIVGNVCLF GAVEGQAYIN GIAGERFAVR NSGATAVVEG
VGDHCCEYMT GGRVVVLGKT GRNFAAGMSG GIAYVFDAQN KFTNGLCNTE TIDFEAVLNE
DAEELKAIIK KHVLYTGSKK GAALLADWDA CLKNFVKVMP IEYKRALERI ETAKPMFEEL
TIA
//
