ID A0A2A4VTU1_9PROT Unreviewed; 1502 AA.
AC A0A2A4VTU1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:PCI61642.1};
GN ORFNames=COB37_08125 {ECO:0000313|EMBL:PCI61642.1};
OS Kordiimonadales bacterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales.
OX NCBI_TaxID=2030814 {ECO:0000313|EMBL:PCI61642.1, ECO:0000313|Proteomes:UP000217879};
RN [1] {ECO:0000313|Proteomes:UP000217879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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:PCI61642.1}.
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DR EMBL; NVTU01000023; PCI61642.1; -; Genomic_DNA.
DR Proteomes; UP000217879; 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}.
FT DOMAIN 24..419
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1502 AA; 163904 MW; 9DA75FA105F830A9 CRC64;
MNSFNQYVPG PIGLYDPADE HSSCGVGLIA KLDGKPDREV VLRGIEALKA IWHRGAVDAD
GKTGDGAGIL LEIPQEFFKT HIRATGHEPD AGRLAIGMVF LPRVDLGAQE TCRTIVETEI
LHFGYTIYGW RQVPVDVSVM GEKAEATRPE IEQIMIANTK GVDDETFERE LYIIRRRIER
SVIEAQVGDF YMCSLSSRSV IYKGLFLAEQ LSTFYPDLLD ENYVSSYAIY HQRYSTNTFP
QWWLAQPFRM LAHNGEINTI RGNVNWMKSH QIRMASMAFG DNSEDIKPVV PTGASDSAAL
DAVFETLVRA GRSAPMAKTM LIPEAWSNKA SMPKAHSDMY AYTNSVMEPW DGPAALAGTD
GKWVFAGLDR SGLRPMRFTV TNDGFLIVGS EAGMVIVDER DVREKGRLGP GQMIALDIEE
GRLYHDKELK DRLAASQPFG EWVKDIKSIY DLPGYKGLED GSYKGENLRR RQIVAGLSHE
DLELILQPQV MTGKEAIGSM GDDTPLAVLS AQYRNLSHFF RQNFSQVTNP PIDSLREQRV
MSLKTRFGNF ANVLDEGHTQ GGALVLDSPV LSNREWQVLI KNFGEEAQII DCTFDVEGGP
NSLRNALIRI RREAEDAVRE GRGHLFLSDE KISAHRAPIP MILATGGLHT HLIQNGLRTF
TSLNVRSAEC LDPHYFAVLI GAGATTVNAY LAQDAIAERQ AKGLFGKQSL TECIIRACSA
IDQGLLKILS KMGISIISSY RGGNNFEALG LSRALVAEFF PGMPTKISGI GLSGVQHKVL
EQHSKAFFEG NNTLPIGGLY RYRRDGEVHG HDGSLIHILQ SAVGNDNYAK YLTYSRGLRN
LPPLNLRDLL DFRRAEEAAS LDEIESITQI RKRFITPGMS LGALSKEAHE TLAIAMNRIG
AKSVSGEGGE DKSRYKPYAN GDNANSPIKQ IASGRFGVTA EYLNACDEIE IKVAQGAKPG
EGGQLPGFKV TEMIAKLRHA TPGVTLISPP PHHDIYSIED LAQLIYDLKQ INPRAKVCVK
LVSSAGIGTI AAGVAKAHAD VILISGHNGG TGASPQTSIK YAGTPWEIGL AEVNQVLTLN
GLRHRVKLRT DGGIKTGRDV VIAAMLGAEE YGVGTAALVA MGCIMVRQCH SNTCPVGICT
QDEELIKKFG GTAEKVVNLF SFIAEETREI LAELGFEKLE DIIGRTELLH QVSRGAGHLD
DLDLNPLLVQ VGGRNQKHIC TLTERNPVPD SLDAQMIEDA KAVFTRGEKM QLTYSVQNTL
RAIGTRFSSE ITQKYGMKGL NPNHVTVRLR GSAGQSLGAF AVQGLKLEVT GDANDYVGKG
LSGGTIVVRP SNHATFNSKD NTIIGNTVLY GATSGKLFAA GQAGERFAVR NSGADVVVEG
CGDNGCEYMT GGTAVILGDA GENFGAGMTG GMAFIYDESG RFEEHVNSET VLLNRLDSAH
WEEVLTGLIT EHATATHSRW ALTLLSNWES KRGQFWQVVP KEMIDRLEFP ISDRAPEKSL
SA
//