ID A0A1H3PVS6_9MICO Unreviewed; 1530 AA.
AC A0A1H3PVS6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:SDZ04509.1};
GN ORFNames=SAMN05216554_2098 {ECO:0000313|EMBL:SDZ04509.1};
OS Herbiconiux ginsengi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Herbiconiux.
OX NCBI_TaxID=381665 {ECO:0000313|EMBL:SDZ04509.1, ECO:0000313|Proteomes:UP000198891};
RN [1] {ECO:0000313|EMBL:SDZ04509.1, ECO:0000313|Proteomes:UP000198891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3491 {ECO:0000313|EMBL:SDZ04509.1,
RC ECO:0000313|Proteomes:UP000198891};
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; FNPZ01000002; SDZ04509.1; -; Genomic_DNA.
DR STRING; 381665.SAMN05216554_2098; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000198891; 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; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
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:UP000198891}.
FT DOMAIN 34..425
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1530 AA; 166436 MW; 235C613897B24098 CRC64;
MADQPAQRST PGFSFSTLPP AQGLYDPSSE KDACGLAMVA TLRGTAGHDI IDTALGALRN
LEHRGAIGSD AGTGDGAGIL TQIPDAFLRA VAPVELPPVG RYAVGNAFLP LHAGERQEVM
DRIRDLAEQE DLRILGWREV PVRPGELGRL ARDAMPAIWQ LFVQSTRTTE SGATLSDLPL
DRQAFRLRKR AELEHQVYFM SLSCRTITYK GMVTTLQLEP FYPDLSDERF ASKLALVHSR
YSTNTFPSWP LAQPLRMMAH NGEINTVQGN RNWMRARQSQ LESELLGDLS PLYPIVTPGL
SDSGSFDEVV ELLTLAGRSL PHAIMMMVPE AWENQADFED ARRAFYEYHS MLMEPWDGPA
ALIFTDGTLA GATLDRNGLR PGRYLITDDG LVVLASEIGV IDVEPSRVVR KGRLRPGKMF
LVDTAAGRLI EDDEIKAELA AAEPYGQWLD EGRINLRDLP EREHIVHTPA SVTRRQRTFG
YTEEEVRILL TPMAKNAAEP LGAMGSDTPI AVLSDRPRLL FDYFTQQFAQ VTNPPLDSIR
EEVVTSLRLG LGPERNLLDA TPEHTRQVIL DFPVIDNDEL AKIQHIDPSS GSRLTTTIKG
LYRVDEGPKA MQNRIAAMCA EADEAIEHGA QFIVLSDRDS NREFAPVPSL LMLAGVHHHL
IRKQTRMKVG LIVEAGDVRE VHHVALLIGY GASAVNPYLA METCENLVRS GDISGVTPEK
AVKNLIKALG KGVLKIMSKM GISTVSSYAG AQTFEAVGLA PEFVEEYFTG TSSKLGGVGI
DVIAGESAAR HAAAYPEDGA TTVHEPLATG GEYQWRREGP PHLFNPDTVF RLQHATRARR
YDIFREYTKL VDDQAENLMT MRGLFKLRTG VRPAVPLDEV ESVESIVKRF STGAMSYGSI
SKEAHETLAI AMNRLGAKSN TGEGGEDVDR LLDPERRSAI KQVASGRFGV TSMYLTHATD
IQIKMAQGAK PGEGGQLPPT KVYPWVARTR HATAGVGLIS PPPHHDIYSI EDLKQLIFDL
KRANPEARVH VKLVSQNGIG AVAAGVTKAL ADVVLVSGHD GGTGASPLNS LKHAGTPWEI
GLAETQQTLM LNGMRDRVVV QVDGQMKTGR DVVIGALLGA EEYGFATAPL VVEGCILMRV
CHLDTCPVGV ATQNPELRAR FSGKPEFVVN FFEFLAQEVR EYLAELGFRS LEEAIGHNEL
LDVNAAIEHF KTDGLDLSPV LVGPHFEPEE PRSNRRPQEH ELEKHFDKRL IHETVAALDH
AEPVAVTLPI RNTERAVGTM LGHEVTKRYG EQGLPDGTIQ ITLLGSAGQS LGAFLPSGIT
LRLEGDSNDY VGKGLSGGQI ILRPDRHSVF PAERNVIAGN VIGYGATRGS MFLRGIVGER
FLVRNSGATA VVEGVGDHAL EYMTGGLALI LGSTGRNLGA GMSGGTAYVY DLHEERVNAD
SLASGELQLL PLGGADVEIV RDLLQRHEAE TGSPLAARML ADFDATIASF VKVLPRDYAA
VLATRQTAVE EGLDPDGDVV WGRILEVTGG
//