ID A0A1I6T390_9BACI Unreviewed; 1510 AA.
AC A0A1I6T390;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glutamate synthase (NADPH/NADH) large chain {ECO:0000313|EMBL:SFS83744.1};
GN ORFNames=SAMN05421668_11238 {ECO:0000313|EMBL:SFS83744.1};
OS Halolactibacillus miurensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halolactibacillus.
OX NCBI_TaxID=306541 {ECO:0000313|EMBL:SFS83744.1, ECO:0000313|Proteomes:UP000199139};
RN [1] {ECO:0000313|EMBL:SFS83744.1, ECO:0000313|Proteomes:UP000199139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17074 {ECO:0000313|EMBL:SFS83744.1,
RC ECO:0000313|Proteomes:UP000199139};
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; FPAI01000012; SFS83744.1; -; Genomic_DNA.
DR STRING; 306541.SAMN05421668_11238; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000199139; 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 22..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1510 AA; 168244 MW; C86E362BF15C02C1 CRC64;
MRFNEKIQAN GMYQPSYERD NCGIGLYANL DGNKSHAIVK NGLDMLTKLD HRGGQGSDPN
TGDGAGLMIQ IPDQYFRKVL PTIDLPEPGD YAVGMFFFQQ HDPHFSAYKS QINQIIKQEK
ETLMTWRKVP TNVEQIGALA KESAPVVYQV FIKRTVAEQG LPFERVLYRM RKQMERFAKG
HDEAFYIPSF SSQTIVFKGL LTSYQVDQFY IDLKDEDVVS HFSLVHSRFS TNTFPSWERA
HPNRYLIHNG EINTLRGNIN KMKAREHNLK ADVFGDDFET ILPILNEDGS DSSVLDNALE
FLILSGKSPQ EAAMMLIPEP YENEETMSED KRAFYRYMSA VSEEWDGPTS MTFTNGKQLG
AILDRNGLRP ARYVITKERD IIYASEVGVL PIDEETIIEK NRLKPGEMLF IDFEQGRIIP
DEEIKESVVT TYPYKNWLAD EVRHITKPQS LTVKKRSDLL SRQRAFGYTH EVIENYLIAL
QEQKKDPIGA MGIDTPLAVL SNKQQSLFHY FKQTFAQVTN PPIDAYRERH VISTKVWLGK
EGDYLNASPD NVRRIELPHP ILTAEELDQL ITLGDDFKSA RLKTTFTNHL SEALTALHEK
AEALIDDGHA LLILTDEDMN EDNVTIPTLL ATSSLHQYLI RQGIRSKVSL IVVSGEVKEA
HHFACLLGYG ADAILPYLVY ETYQQLIEDE TLSQTLTDTI NTYIETMVDG VVKVMSKMGI
STFRSYQGAQ IFEAVGISRD VINQHFTGTT SVLDGITLDV IEQEARMFHE AGFNTSDKRL
PEGSEFQWRH DGESHAYNPA TLTQLQWAAR RGDYHLFKRY TKQMETQHIG FLRHLLDFNE
QVAIDLSEVE PVDSIVKRFK TGAMSYGSIS REAHETLAIA MNRLGGKSNS GEGGEEKDRF
IQTDPLINKM SAIKQVASAR FGVDSDYLVH ANELQIKMAQ GAKPGEGGQL PGDKVYPWIA
NTRRSTPGVD LISPPPHHDI YSIEDLAQLI FDLKNANPKA RISVKLAAKS GVGTISAGVA
KGKADVISIV GYDGGTGASP KTSIKHTGLP LEIGLTEAHQ TLILNGLRQR VTLETDGKLL
TGKDVVMSAI LGAEEFGFAT APLVILGCVM MRVCHLDTCP VGVATQNPAL RERFTGKPED
IENFMRFIAE DMREIMASLG VRTVDELVGQ TQLLKIHERK NLHWKARYLD LSRLLYKPAS
DFCLKKETQA HQLEETLDQA ILYPYFKASI EEKVPQHIKL HVTNIDRATG TTLGYHVTKA
HGEQGLPEDT INIHLSGSSG QSVAAFIPKG MTIHLTGDAN DYAGKGLSGG KLIIEATETM
KPMADQAIIA GNVCFIGATS GEGYINGLAG ERFAVRNSGA NLVVEGVGDN GCEYMTAGQV
VIIGSIGKNF AAGMSGGEAY LYTTNKEATR AYINQELVDL DDSLSNEALN KVKQQLINHK
KLTGSVKAHD ILDNWETEKN HFISVIPRRY KRVTGKIEGF MSTGSTHEEA SLLAFNEIKA
DKIKAGLKVK
//
