ID W4MH72_9BACT Unreviewed; 1532 AA.
AC W4MH72;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:ETX09057.1};
GN ORFNames=ETSY2_01735 {ECO:0000313|EMBL:ETX09057.1};
OS Candidatus Entotheonella gemina.
OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC Entotheonella.
OX NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX09057.1, ECO:0000313|Proteomes:UP000019140};
RN [1] {ECO:0000313|EMBL:ETX09057.1, ECO:0000313|Proteomes:UP000019140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX PubMed=24476823; DOI=10.1038/nature12959;
RA Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT "An environmental bacterial taxon with a large and distinct metabolic
RT repertoire.";
RL Nature 506:58-62(2014).
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:ETX09057.1}.
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DR EMBL; AZHX01000064; ETX09057.1; -; Genomic_DNA.
DR PATRIC; fig|1429439.4.peg.304; -.
DR HOGENOM; CLU_000422_8_2_7; -.
DR Proteomes; UP000019140; 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:UP000019140}.
FT DOMAIN 22..421
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1532 AA; 168445 MW; F6BD5D5937D7A95B CRC64;
MTTPGIPPKQ GLYDPKFEHD ACGIGFVVNI KGVKSHTIVE QALTVLQNLD HRGACGSEEN
TGDGAGVLLQ TPHAFFRAAC TALGFTLPQP GAYGVGMIFL PPEPAPRQSC EQQLEAIVRE
EGQTVLGWRD VPTDNALLGN TAKSCEPFIR QMFIGRSDAL QDEMAFERKL YVIRRRAENT
IRYSGVPGGN AFYIPSLSYK TIVYKGMLTP LQVRAFYPEL SDPSVESALA VVHSRFSTNT
FPSWERSHPY RYLIHNGEIN TLRGNENWMH ARQSQLASEL FGGDLPKLFP IIQEDGSDAA
KFDNCLEFLG LGGRSLAHAM MMMIPEPWEN HDNMDAPKEA FYEYHSSLME PWDGPASIAF
TDGVRVGAVL DRNGLRPSRY YVTKDDLVIM GSEVGVLDVE PERVLEKRRL QPGRMFLVDT
EAGRIISDEE LKREMVTAQP YQQWLERHLV QFDDLPTPPE ETPAYDHQAT LQRLQAYGYS
FEDLRVNIGP MAANGIQPIG SMGTDTPLAV LSDKPQLLYN YFKQLFAQVT NPPIDPIREE
LVTSTTLTIG PERNLLDATP EHCEQIRLSL PVLKNSEMEK LRQLDLPGLQ TVTLPILFKP
VEGTAGLERA LDELYAAADR AIEDGVSILI LSDKGVDRQH AAIPALLASA GLHHHLIRQG
TRTRVGLVLE SGEPRETHHF CLLLGYGVQA INPYMAFESL NDMIHEGLLP DIAYDDAVKG
YIKAVVKGVV KVMSKMGIST IKSYCGAQIF EAVGLGQAFV DTYFTWTPSR VGGIGLAEVA
EEAIRQHAKA FPEFPTNGHT LEVHGQYQYR RNGELHLFNP RTIHTLQKAC RNNDYATFKA
YSELIDDQSE RLSTLRGLFE FKWADEPIPL DEVEPEEAIM KRFKTGAMSY GSISKEAHEA
LAIAMNRIGG KSNTGEGGED PVRYIPDDNG DSRNSAIKQV ASGRFGVTSE YLTQAKELQI
KMAQGAKPGE GGELPGRKVY PWIAKVRLST PGVGLISPPP HHDIYSIEDL AQLIHDLKNA
NHHARISVKL VSEVGVGTIA AGVAKGHADV VLISGHDGGT GASPQTSIKH AGLPWELGLA
ETHQTLVLND LRSRIAVETD GQLKTGRDVV VAALLGAEEY GFATTALVSL GCIMMRVCHL
DTCPVGVATQ NPALREKFMG NPQYAVHFMT FIAREMREIM AKLGFRTVDE MIGRTDKLEV
SRAVNHWKAQ GLDYADILYQ PEVGEDVGRY CQIEQNHGLD KSLDRQVLLD LAAPALERGE
AVKATVPIRN TNRVVGTILG SELTRRVGPE GLPEDTIHFH FQGSAGQSFS AFVPRGITME
LEGDANDYFC KGLSGGKAIL YPSAGSTFTA EHNIIVGNVA FYGATSGEAY IRGMAGERFC
VRNSGVRAVV EGVGDHGCEY MTGGCVVVLG SAGRNFAAGM SGGVAYVFDE DGTFRDHCNL
ETVDIESVSA EELQDIKEMV QRHETYTQSK RAGQLLALWH DVSPKFVKVM PKDFRRMLDA
IQQAEKEGLI GEEAIMMAFE ANKNDVARVS GN
//
