ID A0A0F7JPW9_9DEIO Unreviewed; 1602 AA.
AC A0A0F7JPW9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:AKH16838.1};
GN ORFNames=SY84_06950 {ECO:0000313|EMBL:AKH16838.1};
OS Deinococcus soli (ex Cha et al. 2016).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH16838.1, ECO:0000313|Proteomes:UP000034024};
RN [1] {ECO:0000313|EMBL:AKH16838.1, ECO:0000313|Proteomes:UP000034024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N5 {ECO:0000313|EMBL:AKH16838.1,
RC ECO:0000313|Proteomes:UP000034024};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus soli/N5/whole genome sequencing.";
RL Submitted (JAN-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}.
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DR EMBL; CP011389; AKH16838.1; -; Genomic_DNA.
DR RefSeq; WP_046843409.1; NZ_CP011389.1.
DR KEGG; dch:SY84_06950; -.
DR PATRIC; fig|1309411.5.peg.1418; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000034024; Chromosome.
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:UP000034024}.
FT DOMAIN 43..443
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1602 AA; 175594 MW; C0CF137C4E92F16D CRC64;
MNRTDNRVTP AEAPHTPGTP ASGAELKLAR EQGLYSGAEH DACGVGFVAH IGGRKNHAIV
QQGLKILENL DHRGAVGADP LMGDGAGILI QIPDEFYRAE FAQQGVTLPP LGDYGVGMIF
LPKEIASRRA CEQELERAIV AEGQVVLGWR DVPVNREMPM SPAVREKEPV IRQVFIGAGP
DTLVPDALER KLYVIRRRAS NAIRALNFTH GAEYYVPSMS CRTVIYKGLL LATQVGEYYL
DLQDERVVSA LALVHQRFST NTFPEWPLAH PYRMVAHNGE INTVKGNFNW MRAREGIMAS
PVLGDDLKKL YPISFEGESD TATFDNALEL LTLAGYPMAH AAMMMIPEAW EQNANLDPRR
RAFYEYHASM MEPWDGPAAM VFTDGRQVGA TLDRNGLRPA RYVQTRDDLV ILASESGVLP
VPESKIVKKW RLQPGRMFLI DFEQGRIIED DELKNQFASA KPYAQWVENT RFRLDDSEET
GTVGQFRESL LDRQQAFGYT QEDLKFLMGP MALTGEEGIG SMGNDSPLAV LSGKNKPLFN
YFRQLFAQVT NPPIDPIRES VVMSLVSFVG PRPNLLDINA VNPQLRLEVE QPILDFDDMA
RVRNIEEHTR GKFKAYDLDI TYPAEWGARG VEAKLATINA WAVDAIESGH NIIVISDRRV
DRERVAIPSL LALSSIHHHL VKAGLRMKVG LVVETGDARE VHHFAALAGY GAEAIHPYLA
LETLINLHTD VPGMPALNGI DAHKAIYNYV KAIGKGLSKI MSKMGVSTYM SYCGAQLFEA
VGLKTDFVQK YFYGTPTQVG GIGIFEVAEE ALRNHRGAFS DDPVLAQNLD AGGEYAWRVR
GEEHMWTPDS IAKLQHSVRS GNYATFEEYA RIINDQSKRH MTLRGLFEFK TDGVTPVPLD
EVESASEIVK RFATGAMSLG SISTEAHTTL AVAMNRIGGK SNTGEGGEDP ARYEREMRGE
TLGEGHTLAS ILGESRVEVD YPLEPGDSLR SKIKQVASGR FGVTTNYLTS ADQIQIKMAQ
GAKPGEGGQL PGGKVSEYIG FLRHSVPGVG LISPPPHHDI YSIEDLAQLI HDLKNVNPRA
DISVKLVSEV GVGTIAAGVA KAKADHIVIA GHDGGTGASP WSSIKHAGSP WELGLAETQQ
TLVLNRLRDR VRVQTDGQLK TGRDVVIAAL LGADEFGFAT APLVAQGCIM MRKCHLNTCP
VGVATQDPVL RARFQGKPEH VINFFFFIAE EVRAIMASLG IRSFDDLIGR ADLLDTKKGI
EHWKAQGLDF SRVFYRPEVP GEVGVRHLHT QDHGLSGALD LQLIEKCRPA FEKGEKVHFL
QDVRNVNRTV GAMLSGELTR VRPEGLPDNT VFVQMEGTGG QSFGAFLAPG LTLYLIGDAN
DYTGKGLSGG RVVVRPSIEF RGKAEENIIV GNTVLYGATS GEAFFRGVAG ERFAVRLSGA
EAVVEGTGDH GCEYMTGGTV VVLGQTGRNF AAGMSGGVAY VYDVDGQFEK RCNTSMVDLH
PLLPEDQQFA QTQGGLHFDQ SDEAHLRRLL ESHHKWTGSQ RASELLDDWD TTLKRFVKVF
PKEYQRALRE RAQAGTVQAA DTTSMQTAQP GNPVAAQGTL TK
//
