ID A0A0M0KQC7_9BACI Unreviewed; 1490 AA.
AC A0A0M0KQC7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KOO41046.1};
GN ORFNames=AMD01_19000 {ECO:0000313|EMBL:KOO41046.1};
OS Priestia koreensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO41046.1, ECO:0000313|Proteomes:UP000037558};
RN [1] {ECO:0000313|Proteomes:UP000037558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14210 dsm16467.";
RL Submitted (AUG-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:KOO41046.1}.
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DR EMBL; LILC01000030; KOO41046.1; -; Genomic_DNA.
DR RefSeq; WP_053403029.1; NZ_LILC01000030.1.
DR STRING; 284581.AMD01_19000; -.
DR PATRIC; fig|284581.3.peg.4177; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000037558; 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; cd02808; GltS_FMN; 1.
DR CDD; cd00504; GXGXG; 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:UP000037558}.
FT DOMAIN 22..391
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1490 AA; 162546 MW; 7A8E920B6D201F80 CRC64;
MRQSTWTPSL FKDYHLHEHD ACGIVSVIEK EREATKKNIE DCINALNTMN HRAGFVNGEG
DGIGVHIDLP TILWKEKLSK AGLNESLVDQ DSFIVGHFFI SKEVSKTSAK KRILSVLEGL
NFELVYEADN ITNSDVLGPL AKNEEPYFWQ VGLISKDTHS IKKKTFEATL EIEKDAAVHV
SSLSNSYVVY KVMGAGDTLK AYYEDLKSPV IASTMTLGHN RYSTNTLTNF FRVQPFSLLG
HNGEINTVAK LRDEARMMNV SLTNGGSDSQ DLDRIIQSLI SRDDYSLFEA VDVLFPPIVN
EIKAYPPHLQ DLYTYVREAW GHFAQGPAGI ISRYEDEAVF SVDSLGLRPL WKLETESSYL
FSSEPGIIPN GEYVAEPKPL GPGEKVGLKW NADGKMVVFD YPALQQEVYE RFSKRIKLTD
DRLRLSTPHY PTNVLMTNLG KVSNGHYAAF GWDREHIQLI EQMADNGAEP IRSLGHDAPL
AALHGGRKNI ADYIKESVAV VTNPAIDRDR ETEHFSTRVI VGKRPSLSKK EDNDYVVELL
SPILIEGEQG NRCAESLEQP SFDQLVNDYQ QKQLSYYLSA TFKNGESIPE ALKRLEEEAT
EAVLGGKTLL IIDDAQAHQN GQYFLDPHLV TAALDQALVE KQLRRDCTLL LRSGAIRSLH
DVVTAFGLGA NVISPYLLFA TVFEETDQPT LNLYSALIKG LEKVISTIGI HELRGYGRLF
SAIGLHDDIA GILNVVNFFG STTLVHDWEQ MKEDSIARAS EYEDEKARPG KTFHLFPRIW
KAIGEVAQTG SYDAYREKLT EQEEGNPTTI RHLTNITSSP KRVSPEKVDV GVGEHSLPFV
IASMSFGSQN EIAFRAYAEA ANRLNMVSLN GEGGEIKDML GKYPRTRGQQ VASGRFGVNA
ELLNSSNLLE IKIGQGAKPG EGGHLPASKV TLKIAEARNA TVGSDLISPS NNHDIYSIED
LAQMISELKT ANDQAKVAVK VPVVPNIGTI AVGIAKAGAD IITLSGFDGG TGAARIHALQ
HVGLPVEIGV KAAHNALLEA GLRQKVEIWA DGGIKSALDV VKMMMLGANR IGFGTLSMIA
IGCTTCRGCH LDTCHVGIAT QIESEAQAKE HGLRRFVPRQ LDNAVQGLTN LFTAFGNELK
QLAGDLGFDR LQDLVGRSDL LTQARGKDLL DLTYLLKTVD IQPFAQPEVA ASVEEEQLSV
AVGSEYLDYH VESLEKSRSY DTVTSEQRIL GSRVSCHRVR NRLDGSYKKL PAISLQYNNG
SIPGNGLGAY NTSGINIQVS GGAQDGTGKT SFGGSISILK SPGKNGGYYN GSVGKGFGYG
AQSGLLLAQG NADARAGIRL SGADMIIGGK VVSPIPEEEH GNIGVNANIK GFAFEYMTNG
RGLVMGDPGP WICAGMTGGV VYLRHQPEMG LTKEALKRRI AKGAKVDLSP LNAKGLADVK
ELLTLYSNEL TNQGQLDEAK EIEKLASNPS AYFLQVIPSK EQADPSVSTE
//
