ID A0A1G6UTW5_9SPHI Unreviewed; 1505 AA.
AC A0A1G6UTW5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:SDD44731.1};
GN ORFNames=SAMN05216464_101757 {ECO:0000313|EMBL:SDD44731.1};
OS Mucilaginibacter pineti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDD44731.1, ECO:0000313|Proteomes:UP000199072};
RN [1] {ECO:0000313|EMBL:SDD44731.1, ECO:0000313|Proteomes:UP000199072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47C3B {ECO:0000313|EMBL:SDD44731.1,
RC ECO:0000313|Proteomes:UP000199072};
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; FNAI01000001; SDD44731.1; -; Genomic_DNA.
DR STRING; 1391627.SAMN05216464_101757; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000199072; 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:UP000199072}.
FT DOMAIN 20..420
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1505 AA; 165548 MW; E444ED3635B71DBF CRC64;
MNQTESHQGL YRPEFEHDSC GTGFITNING HKSNQIIDDA LTMLENMEHR GACGCDPETG
DGAGILIQLP HEFFMEECSN LEISLPEPGE YGVGMIFFPK DSAAKKACRI VITNAIEKLG
LHKLGYRKLT VDSMAVGETA RQAEPDVEQI FISRPHHITN ADDFERKLFI LRRYINKTIT
ETIPAAAEHF YFTSLSCKTI VYKGQVTTYQ LRKYYSDLTD PRIASGFAMI HSRFSTNTFP
SWKLAQPFRL IAHNGEINTL TGNLNWFYSG LKSYASAYFT ADEMEMIMPV IDNNQSDSAC
LDNIIEILLH SGRSLPHVMM MLIPEAWDGN EQMDPVKKAF YEYHATLMEP WDGPAAISFT
DGKLVGAVLD RNGLRPLRYV ITNDGRVIAA SEAGTLTIDE STIVRKGRLQ PGKMLLIDTE
KGRIITDDEI KKQISSQQPY GRWLENYKIN LSELTEPRLA FASLSEASVF RYQQVFGYSR
EDIDTIIKPM AVDGKEPIGS MGTDVPLAIL SDKPQHLSSY FKQFFAQVTN PPIDPIRERL
VMSLATFIGN NGNLLDEDKM HCHCVVLKHP ILKNHQLEKL RSIDTGLFHA KTLQTYFVAD
GMPGSLEKGI ARLCRYAEDA VDDGFEVLIL SDRAVDSEHA PIPTLLAVSA VHHHLIKKGR
RGSVGLVVET GDAWEVHHFA CLLAFGATAI NPYLALATIE TVKNNGSLET SYDLKKLQSN
YVKSVNDGLL KIFSKMGIST LQSYHGSQVF EILGLNKAVV DKYFSGAVTR IGGLGLDEIA
REALCKHRMG FNAKGGDNLL PEGGIYQWKR RGEAHLFNPT TVHLLQHATR SNDYAVYKNY
AKVINEQGEK HFTIRGLLDF AHHREAISID EVEPAENIMK RFATGAMSFG SISHEAHSTM
AIAMNRIGGK SNTGEGGEDE MRYEQMANGD SMRSAIKQVA SARFGVTSNY LTNADELQIK
MAQGAKPGEG GQLPGHKVDD WIAKTRHSTP GVGLISPPPH HDIYSIEDLA QLIFDLKNAN
RTARINVKLV SKAGVGTIAA GVAKAHADVI LIAGYDGGTG ASPISSVKHA GLPWELGLTE
AHQTLVRNKL RSRVVLQTDG QLKTGRDLAI ACLMGAEEWG VATAALVAGG CIMMRKCHLN
TCPVGVATQD PELRKLFSGK ADHVVNLFRF MAEELREIMA ELGFRTINEM VGRVQFLKVK
DNLQSWKAKK IDLSGILHPV TNTKGMTLYN SESQDHGMSE IIDWKLLESA KAALEDKTPV
FASFDVINVN RTIGTLLSNE ISKIYGSAGL PDNTINYKFK GSAGQSFGAF ATKGISFELE
GEANDYVGKG LSGAQLAIYP AQNATFAPQD NIIIGNVALY GATSGELFVG GMAGERFAVR
NSGATTVVEG IGDHGCEYMT GGRALILGQT GRNFAAGMSG GLAWIYNPEN NFAENCNTEM
VDLDPLSLQD EEQIKGLLKK HISLTGSKLA QQILTNWAEA STQFVKVYPK EYKKVVEKLQ
YQTIG
//
