ID A0A0M8WHQ1_9NOCA Unreviewed; 1524 AA.
AC A0A0M8WHQ1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KOV85910.1};
GN ORFNames=ADL03_09655 {ECO:0000313|EMBL:KOV85910.1};
OS Nocardia sp. NRRL S-836.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV85910.1, ECO:0000313|Proteomes:UP000037746};
RN [1] {ECO:0000313|Proteomes:UP000037746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KOV85910.1}.
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DR EMBL; LGDY01000089; KOV85910.1; -; Genomic_DNA.
DR STRING; 1519492.ADL03_09655; -.
DR PATRIC; fig|1519492.3.peg.2077; -.
DR Proteomes; UP000037746; 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:UP000037746}.
FT DOMAIN 39..427
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 919..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1524 AA; 165897 MW; 935B6EA67969C47F CRC64;
MSTRTSSSAR TTKEVCAVIF SAIPGPQGLY DPADERDACG VAMVADIQGR RSHGIVSDAL
TALANLEHRG AAGAEPTSGD GAGILLQLPD EFLRAVVEFD LPERGGYAAG IAFLPFEAEE
REAARQQIER IAVEESLEVL GWREVPVDPE KANVGPTALS VAPHFAQLFV KGTRGETGIE
LDRLTFCLRK RVEHEGSVYF PSLSSRTIVY KGMLTTEQLP AFFPDLHDER LYTAIALVHS
RFSTNTFPSW PLAHPFRFVA HNGEINTVRG NRNRMRAREA LLDSDLIPGD LARLFPICDP
DGSDSASFDE VLELLHLGGR SLPHAVLMMI PEAWENHATM DPKRRAFYQF HASLMEPWDG
PACVTFTDGE LVGAVLDRNG LRPARWWQTA DGRVVLASES GVLDVPSDQV VAKGRLQPGR
MFLVDTTQGR IVDDEEFKSG LATEQPYDEW LHAGLLDLAD LSDREHVVQS HESVVRRQLT
FGYTEEELRI LLTPMSVAGM EPLASMGTDT PVAALSQRSR LLYDYFVQNF AQVTNPPLDA
IREEIVTSVK RVMGPEQNLL DPGPVSCRHV TLDYPVIDND ELAKLIHIND DGDLPGFACT
VLSGLYEVDG GGEALTAAIE RVRREASEAI ANGARTLVLS DRDSDHRMAP IPSLLLVSAV
HHHLVRTKER LRVALVVESG DCREVHHVAA LLSYGAAAVN PYLAFETIED LISQGAITGV
PAHKAIRNYV KALVKGVLKI MSKMGISTVG AYTAAQIFEA VGLSNDLLDE YFTGTQSKLG
GVGLDVLAEE VALRHRRAYP DNPTDRAHRR LEVGGEYSYR REGELHLFTP ETVFLLQHAT
KTRKEDVFRQ YTAEVERISR QGGTLRGLFK FRTGGRTPIP IDEVEPVSSI VKRFNTGAMS
YGSISAEAHE TLAIAMNRLG GRSNSGEGGE DRERLYDPQR RSAVKQVASG RFGVTSEYLV
NSTDIQIKMA QGAKPGEGGQ LPGFKVYPWV ARTRHSTPGV GLISPPPHHD IYSIEDLAQL
IHDLKNANEQ ARVHVKLVSS IGVGTVAAGV AKAHADVVLI SGYDGGTGAS PMNSLKHAGT
PWEIGLAETQ QTLLLNGLRD RITVQVDGAM RTGRDVVVAA LLGAEEFGFA TAPLIVAGCV
MMRVCHLDTC PVGVATQNPD LRARYTGQAD HVVNFFEFIA QEVRELLAEL GFRTIDEAVG
HAELLDKDEA IEHWKTAGLN LDPVFEVPDT PYPTAKRRVR DQDHGLDKAL DRTLIQLAEA
ALEDAHQVTL ELPVRNVNRT VGTLLGAEVT RRYGGEGLED DTIRVKLTGS AGQSLGAFLP
RGITLEMVGD ANDYVGKGLS GGRIIVRPHD DAPFRAEDQV IAGNVIGYGA TSGEIFLRGR
VGERFCVRNS GATLVAEGVG DHAFEYMTGG RAVVLGPTGR NVAAGMSGGI AYVLDLDPLS
VNQEMVQLQR LSAEDLRWLK DVVTRHHELT GSAVAASLLG DWTRRAGAFT KVMPGDYQRV
LEAMRLARAE GRDVDAAVME ASRG
//
