ID A0A238Z380_9FLAO Unreviewed; 1503 AA.
AC A0A238Z380;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:SNR77339.1};
GN ORFNames=SAMN06265371_11234 {ECO:0000313|EMBL:SNR77339.1};
OS Lutibacter agarilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1109740 {ECO:0000313|EMBL:SNR77339.1, ECO:0000313|Proteomes:UP000198384};
RN [1] {ECO:0000313|EMBL:SNR77339.1, ECO:0000313|Proteomes:UP000198384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29150 {ECO:0000313|EMBL:SNR77339.1,
RC ECO:0000313|Proteomes:UP000198384};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FZNT01000012; SNR77339.1; -; Genomic_DNA.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000198384; 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:UP000198384}.
FT DOMAIN 16..411
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 898..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1503 AA; 167648 MW; 94BB032D24AA1F82 CRC64;
MIKQGLYLPE FEHENCGAGF ICNLKGQKTN QIIHDALEIL VKLEHRGGVS SDGKTGDGAG
LLIDIPHEYF LRVCDFELPA QRDYAVGMVF FPKNVNQYRF CKEEFEKEIK NQGLKILGWR
TVPVDSSQLG QIALDSEPTI EQVFIGKGRI KKELNFKAKL YAARKITEHT IAGSKMSEAS
YFYVSSLSNT TLIYKGIIMP EDIGPYFIDL QQPDLVTRLA LVHQRFSTNT MPSWELAQPF
RYMCQNGEIN TLRGNVSRMR IREEIMKSDL FGDDIEKLFP IVLPGKSDSA SMDMVVELLS
LTGRSLPEVM MMLIPEAWEK HKTMSPERKA FYEYNACLME AWDGPASVPF TDGDYIGALL
DRNGLRPSRY TVTKSGKLIM SSEIGVVDID PEDVERHGRL EPGKMFLVDM NKGRIINDEE
IKNKIVNERP YKAWLDETRI HLKDVENTNE DCPIETLDIR TRSRLYNYTI EDIQEVITPM
AQNGKEALGS MGIDTPLAVL SDRPQLISNY FKQLFAQVTN PPLDGIREEI VTDISLALGK
DRNIFSISQR QCKKLRIQNP VISNNDLEKI RNIKIGRDFK AITIQMLYKK EQGVNGLEDA
LENIITQVSK AVDKRNNIII LSDRGANEEM APIPALLACS YVNHEMNRLR KRSYFDIVIE
SAEPREPHQF ATLFGYGASA INPYMVNEII RLQVKEGFIT GMDEQKAVDN FNKAIGTGLL
KIMNKIGIST LHSYRGSQIF EIVGFNSKFV EKYFPYTASR IEGVGLYEIE KEISARYNYA
YPKTLIKNRL GLNIGGHYRW RRGGEKHMFN PTTVAKLQQA VRLSDQASYD VYAKTVNEQS
ERLMTIRGLF EFNNFDPIPI EEVEPWTEIV KRFKTGAMSY GSISREAHEN LAIAMNRIGG
KSNSGEGGED RKRFQKDING DSRNSAIKQV ASGRFGVTSH YLTNAEEIQI KMAQGAKPGE
GGQLPGEKVL PWIAEARNST PFVGLISPPP HHDIYSIEDL AQLIFDLKNA NREARINVKL
VSEVGVGTIA AGVSKAKADV VLISGYDGGT GASPLTSLKH AGLPWELGLA EAQQTLVLNN
LRSRIVVECD GQLKTGRDVA IAALLGAEEF GFATAPLVAS GCIMMRKCHL NTCPVGIATQ
DKSLRKNFKG TPEHVINFFY YVAEELRGIM AQLGFRSMAE MVGQTQKIDS NKAIKHYKAK
GLDLSSILHR PAGYSEMPLK NTEKQDHDID NVIDFQILND SHRAIYRKEK TTLEYPICNI
DRSTGAITSN EISKIYGHLG LPEDTLNINF TGSAGQSFGA FGAPGLTFTV EGNTNDYLGK
GLSGAKLIVK KPAKATFIAE DNIIIGNVCL FGAVKGEAYI NGIAGERFAV RNSGAISVVE
GVGDHCCEYM TGGKVIVLGG TGRNFAAGMS GGIAYVYDPK DKFTNGLCNT ETIEFEQIEK
DEAAELKALI EKHVLYTNSN RGKELLKDWD NSLGNFVKVM PIEYKRALKR LETEEPMVEE
LTA
//
