ID   A0A2A4E4F2_9MICO        Unreviewed;      1530 AA.
AC   A0A2A4E4F2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:PCE13756.1};
GN   ORFNames=AUC47_08150 {ECO:0000313|EMBL:PCE13756.1};
OS   Microbacterium sp. SZ1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1849736 {ECO:0000313|EMBL:PCE13756.1, ECO:0000313|Proteomes:UP000217958};
RN   [1] {ECO:0000313|EMBL:PCE13756.1, ECO:0000313|Proteomes:UP000217958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZ1 {ECO:0000313|EMBL:PCE13756.1,
RC   ECO:0000313|Proteomes:UP000217958};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-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:PCE13756.1}.
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DR   EMBL; LPVV01000040; PCE13756.1; -; Genomic_DNA.
DR   Proteomes; UP000217958; 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}.
FT   DOMAIN          34..425
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1530 AA;  166465 MW;  6E0D6EF4093E1B02 CRC64;
     MRTVQVYFQP PHGASGAYPP KQGMYNPAFE KDACGLAMVA TLRGEAGHDI IALALEALRN
     LEHRGAIGSD AGTGDGAGIL TQMPDAFLRA VTDFELPPMG EYAAGLAFLP RDSSVRREQK
     AGIERIARSE GLRVLGWREV PTANEHLGKL ADEARPAFEQ LFVSAGGASH SDAPLTGIAL
     DRVAYRLRKR AGHELGAYFV TLSARTLGYK GMVTTLQLEP FYPDLQDERF MSELAVVHSR
     YSTNTFPSWP LAQPLRMLAH NGEINTVGGN RNWMRARQSQ LESELLGDVS PLLPICTDGA
     SDSASFDEVL ELLTLTGRSL PHAIMMMVPE AYEKQSDISP ELRAFYEYHS NQMEPWDGPA
     ALIFTDGTLV GATLDRNGLR PGRWTETTDG LIVIGSETGV LTFEPERIKR RGRLQPGKMF
     LVDTAQQRII EDEEIKRDLA TMHPWQEWLD AGAVRLADLP EREHIVHPPA SITRRQRTFG
     YTEEEVRILL TPMGQTGVEP LGAMGSDTPI AVLSKRPRLL FDYFTQQFAQ VTNPPLDSIR
     EEVVTSLKLG LGPESNLLSW GPDHTRTVSL DFPVIDNDEL AKIRHIDKAL PDRSSVTIKG
     LYHFDVGSNT LEKRLTEMCD EVDEAIASGA EFIILSDRDS NKDLTPIPSL LMVSAVHHHL
     IRRENRMKVG LIVEAGDVRE VHHVATLIGY GASAINPYLA METVEHLVRT GYITGISPEK
     AVKNLIYALG KGVLKIMSKM GISTVSSYAG AQVFEAVGLS EEFIDKYFTR TESKLGGIGI
     EEIFAENQAR HDYAYPEDAA ARAHERLWSG GEYQWRRDGS PHLFNPETVF KLQHSTRERR
     YDIFRQYTKL VDDQAAELKT LRGLFALRTG TRKPVPIDEV EPVSAIVKRF STGAMSYGSI
     SKEAHETLAI AMNRLGGKSN TGEGGEDVDR LMDPERRSAI KQVASGRFGV TSLYLTEADD
     IQIKLAQGAK PGEGGQLPPQ KVYPWVARTR GGTPGVGLIS PPPHHDIYSI EDLKQLIFDL
     KRANPDARIH TKLVSQSGIG AVSAGVAKAL SDVILVSGHD GGTGASPMNS LKHAGTPWEL
     GLAETQQTLM LNGMRDRVVV QVDGQLKTGR DVIIGALLGA EEFGFATAPL VVSGCIMMRV
     CHLDTCPVGV ATQNPVLRER FTGKPEFVVN FMEFIAEEVR EILAELGFRS LDEIIGRAEL
     LEVDAAVEHW KAEGLDLSPV LEGPAFPASE PRRSRRAQDH ELDKHFDVQL IDIAGPALLN
     GEPVIAELPI ANTERAVGTM LGHQVTSRHG ADGLPRGTID VTLHGTAGQS LGAFLPSGIV
     LRLEGDANDY VGKGLSGGDI TIRPPRGSHI APHENVIAGN VIGYGATAGT MFLSGVVGER
     FLVRNSGATA VVEGVGDHAL EYMTGGVAVI LGTTGRNLGA GMSGGVAYIR SLDTGKINAQ
     SLSSGELLLE PLDRADLEVL RSLIAEHVER TASPLGSDIL ARFDEVAGQF TKVLPRDYAA
     VRSMREEAVA EGIDPDGDVV WNRILEVTGG
//