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Database: UniProt
Entry: A0A2A4VTU1_9PROT
LinkDB: A0A2A4VTU1_9PROT
Original site: A0A2A4VTU1_9PROT 
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
//
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