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Database: UniProt
Entry: A0A1H3PVS6_9MICO
LinkDB: A0A1H3PVS6_9MICO
Original site: A0A1H3PVS6_9MICO 
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
//
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