ID A0A0C5VIC2_9GAMM Unreviewed; 1484 AA.
AC A0A0C5VIC2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glutamate synthase domain 2 {ECO:0000313|EMBL:AJQ93103.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:AJQ93103.1};
GN ORFNames=YC6258_01055 {ECO:0000313|EMBL:AJQ93103.1};
OS Gynuella sunshinyii YC6258.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Gynuella.
OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ93103.1, ECO:0000313|Proteomes:UP000032266};
RN [1] {ECO:0000313|EMBL:AJQ93103.1, ECO:0000313|Proteomes:UP000032266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ93103.1,
RC ECO:0000313|Proteomes:UP000032266};
RA Khan H., Chung E.J., Chung Y.R.;
RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT YC6258T gen. nov., sp. nov.";
RL Submitted (JAN-2014) 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; CP007142; AJQ93103.1; -; Genomic_DNA.
DR RefSeq; WP_044616002.1; NZ_CP007142.1.
DR STRING; 1445510.YC6258_01055; -.
DR KEGG; gsn:YC6258_01055; -.
DR PATRIC; fig|1445510.3.peg.1031; -.
DR HOGENOM; CLU_000422_8_2_6; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000032266; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:AJQ93103.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032266}.
FT DOMAIN 15..406
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1484 AA; 162416 MW; 38ED495DC2944C79 CRC64;
MHAGLFNPQE FRDNCGFGLL AHMQGQASHE LLQTAIESLT CMTHRGGIAA DGKTGDGCGL
LIQRPDAFLR SEAKALFNVE LGERYAVGMV FMHPDTAIYS KGKAALAQTL TDQGLEVVGW
REVPVNPDCL GPMALACMPR IEQIFVVGSG LSEQQFAVKL FTARRKAEIA VEENSDHFYI
CSLAEQVLSY KGLMMPVDLP SFYPDLGNPL VETAIVVFHQ RFSTNTMPRW PLAQPFRFLA
HNGEINTIQG NRNWARARAP KFQTDLLPNL EELQPVVNIT GSDSSSMDNM LDLLLTGGMD
VFRAVRTMIP PAWQNVEHID SDLKAFYELN SMHMEPWDGP AGVVLTDGRY AICLLDRNGL
RPARWMIHKN GYITLASEIG VWNYKPEDVI SKGRVGPGRI MAVDTHTGEF LETEEIDNRL
KSRYPYKQWL KKHAVRLRSN LQHSEEAEGA SLSAEQLSIH QKMFQVTREE REQVLRSLAE
TGQEAVGSMG DDAPMAVLST RVRPMTDYFR QQFAQVTNPP IDPIRESIVM SLETCLGPER
NLFNVTEDCA RRFILSSPVL SPMKYQALLH IDREEFSHRV IDITYDASQE VLKDAVIRIA
DLAEQASREG VAIVILSDRN IEAGRLPVPA AMATGAAHHR LVDKGLRCNT NVVLDTGAIR
DPHQFAVVIG FGATAVYPYL AYEVLDNMIK AGDLIGNPTA LYKNYRKGID KGLFKIMSKM
GISTVASYRG AQLFEAVGLS SEVVGICFKG VTSRIEGARF EHFEQDLKLL AKDAFKARKP
IRTGGLLKYV HDGEYHAFNP DVVMAIQDAV QNNDAGRYRD FAALVNERHP ATLRDLFALN
PQKRIPVSEV ESAESLLKRF DTAAMSLGAL SPEAHEALAV AMNEMGGRSN SGEGGEDPAR
HGTIKRSKIK QVASGRFGVT AEYLVNAEVI QIKVAQGAKP GEGGQLPGGK VNKLIATLRF
AVPGVTLISP PPHHDIYSIE DLAQLIFDLK QVNPEALISV KLVSEPGVGT VAAGVAKAYA
DLITISGYDG GTAASPLTSI KHAGSPWELG LSEAHQTLRG NDLRDKVRLQ TDGGLKTGMD
VIKAAILGAE SFGFGTIPMV ALGCKYLRIC HLNNCATGVA TQDDALRANH FRGTVEMVKN
YFHFVAEEVR ELLAELGFRT LEEIIGHTEL LTAKKGVTDR QACLDLSPIL FSDPVMKDKP
HTVQVHRNQP FDQGEKAEQM VAEVLPAIAE KSGGTFSFDV CNCDRSIGAR VSGEIARRYG
NQGMVGQPIT LNLSGVAGQS FGVWNAGGLH MILDGDANDY VGKGMTGGKL VIRPPKGSSF
STQETSIIGN TCLYGATGGH LYAAGTAGER FAVRNSGAHA VVEGAGDHCC EYMTGGMVAV
LGKTGGNFGA GMTGGFAFVL DLDNRFPDRY NRELVDIHRV SSEAMEDYRK YLYEVVAQHT
EETRSAWGAE LLDNFDDYVY RFWLVKPKAA SLEQLLSSTR ARPE
//
