ID A0A1K2IDU6_9FLAO Unreviewed; 1504 AA.
AC A0A1K2IDU6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:SFZ90569.1};
GN ORFNames=SAMN05428642_1011013 {ECO:0000313|EMBL:SFZ90569.1};
OS Flaviramulus basaltis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flaviramulus.
OX NCBI_TaxID=369401 {ECO:0000313|EMBL:SFZ90569.1, ECO:0000313|Proteomes:UP000182544};
RN [1] {ECO:0000313|EMBL:SFZ90569.1, ECO:0000313|Proteomes:UP000182544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18180 {ECO:0000313|EMBL:SFZ90569.1,
RC ECO:0000313|Proteomes:UP000182544};
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; FPKV01000001; SFZ90569.1; -; Genomic_DNA.
DR STRING; 369401.SAMN05428642_1011013; -.
DR Proteomes; UP000182544; 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:UP000182544}.
FT DOMAIN 17..412
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 898..923
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 1504 AA; 167927 MW; 07B3041EA3FBCF3A CRC64;
MLKKQGLYLP EFEHENCGAG FICNLKGEKT NQIIHDALEI LVKLEHRGGV SADGKTGDGA
GLLIDIPHEY FLRVCDFKIP DPREYAVGMV FLPKTENQHR FCKDVFEKEI KAQGLAVLGW
RKVPVDSSQL GEIAKASEPN IEQIFVGKTE AIDEAVFKAK LYAARKITEH TIRRSKISES
GYFYLPSLST TTLIYKGIIM PEDIGPYYTD LQQIDLVTRL ALVHQRFSTN TMPTWELAQP
FRFMCQNGEI NTLRGNVSRM RVREEIMKSD VFGPQIDKLF PIILPGKSDS ASMDMVVELL
THTGRSLPEI MMMMIPEAWE KHKTMSEERK AFYEYNGCIM EPWDGPASVP FTDGDYIGAL
LDRNGLRPSR YTVTKSGKLI MSSEIGVVDI APEDIESHGR LEPGKMFLVD MNEGRIIKDE
EIKSKIVLER PYKEWLDKTR LHLKDVPYTN ETCPIETIDI KTRQRLFNYT FEDIQEVITP
MAIVGKEALG SMGIDTPLAV LSDRPQLISN YFKQLFAQVT NPPLDGIREE IVTDIGLNLG
KDRNIFSITE RQCRKLKIQN PVISNADLEK IRTIDIEGFK AETINILYPK SQGVNGLEDA
LENIIKQVEK ALVRKTNIII LSDRGVNQDF APIPALLACS YVNHQMNRLR KRSYFDIIIE
SAEPREPHHF ATLFGYGASA INPYMVNEII RMQVKDGFIT GIDEQKAVDN FNKAIGKGIL
KIMNKIGIST LHSYRGSQIF EIVGFNSRFV EKYFPYTASR IEGIGLYEVE KEINERYKSA
YPDKAIDKLL GLNIGGDYRW RRNGERHLFN PTTVAKLQQA VRLSDQASYD VYSQAINEQA
ENLMTIRGLF EFDNLDPIPI DEVEPWTEIV KRFKTGAMSY GSISREAHEN LAIAMNRIGG
KSNSGEGGED RKRFHPDVNG DSRNSAIKQV ASGRFGVTSH YLTNAREIQI KMAQGAKPGE
GGQLPGEKVY PWIAAVRNST PFVGLISPPP HHDIYSIEDL AQLIFDLKNA NRDARINVKL
VSEVGVGTIA AGVAKAKADV VLISGYDGGT GASPLTSLKH AGLPWELGLA EAQQTLVLNN
LRSRIVVECD GQLKTGRDVA IAALLGAEEF GFATAPLVAS GCIMMRKCHL NTCPVGIATQ
DKELRKNFKG TPEHVINFFF YIAEELRGIM AQLGFRTLGE MVGQTHKINA NKAIKHYKAK
GLDLSSILYR PTAYRQMIVK NTEQQDHNLD NVLDFTILKD SHRALYRKEK MTLAYPIRNI
DRTVGAIVSN EISKIYGHLG LPEDTLNINF TGSAGQSFGA FGAHGLSFTI EGNTNDYLGK
GLSGAKLIVK KPVKADFIAE ENIIIGNVCL FGAVQGEAYI NGIAGERFAV RNSGAIAVVE
GVGDHCCEYM TGGKVVVLGK TGRNFAAGMS GGFAYVYDPE NKFVNGLCNT ETIDFEDISI
EDSLELKGLI QKHVLYTDSN RGKELLDNWE TSLNNFVKVM PTEYKRALKR LETEEQMVEE
LTIA
//
