ID R6MQT0_9BACE Unreviewed; 1130 AA.
AC R6MQT0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Class II glutamine amidotransferase {ECO:0000313|EMBL:CDC01120.1};
GN ORFNames=BN659_01321 {ECO:0000313|EMBL:CDC01120.1};
OS Bacteroides sp. CAG:443.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262739 {ECO:0000313|EMBL:CDC01120.1, ECO:0000313|Proteomes:UP000018098};
RN [1] {ECO:0000313|EMBL:CDC01120.1, ECO:0000313|Proteomes:UP000018098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:443 {ECO:0000313|Proteomes:UP000018098};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDC01120.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CBEN010000133; CDC01120.1; -; Genomic_DNA.
DR AlphaFoldDB; R6MQT0; -.
DR Proteomes; UP000018098; 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:0016740; F:transferase activity; 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; 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.
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 ECO:0000313|EMBL:CDC01120.1}; 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 Transferase {ECO:0000313|EMBL:CDC01120.1}.
FT DOMAIN 1..57
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|Pfam:PF00310"
FT DOMAIN 84..367
FT /note="Glutamate synthase central-N"
FT /evidence="ECO:0000259|Pfam:PF04898"
FT DOMAIN 429..800
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
FT DOMAIN 878..1065
FT /note="Glutamate synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01493"
SQ SEQUENCE 1130 AA; 123953 MW; 73C38650AF1D27DD CRC64;
MVVASETGTI SFNPDEIEAK GRLQPGKILL VDTQEGKIYY DNEVKENLAS ALPYTEWLSA
NRIELDTLRS GRKVENSVKN AGRRLRIFGF TREDVERTLT PMCKTGAEPT ASMGNDTPLA
VLSEKPQLLF NYFRQQFAQV TNPAIDPIRE ELVMSLTEYI GAVGKNILTP DPMHCKMVRL
PHPILTNTQL DILCNIRYKG FSTVKLKMIF DIKDGEEGLR SAIEDLCKKA EEAVDAGANY
IVLSDRDIDA THAPVPSLLA VSAVHHHLIS VQKRVQTALI VESGEAREVM HAALLLGYGA
SAICPYMAFA VIDGLVKKGD VQLDYNTAEK NYIKALCKGL YKVMSKMGIS TIRSYRGAKL
FEAVGLNAEM MKRYFGTDIS TIGGAGLKDI ASDYLKFHES GASISEDEAA SMLDNIGLFS
YRKDGEKHAW NPETISLLQL ATRTGSYKKF KEFTQKANEK ESPVFLRDFF RFRNNPIDIN
TVEPVESIVK HFVTGAMSFG AISKEAHEAM ALAMNKLGAR SNTGEGGEDS ERFKAVYHSN
ADNEDISLCS KTKQIASGRF GVTTEYLVNA EEIQIKVAQG AKPGEGGQLP GFKVDEVIAR
TRHSIPGISL ISPPPHHDIY SIEDLAQLIF DLKNVNPRAA ISVKLVAESG VGTIAAGVAK
AKADLIVISG AEGGTGASPA SSMRYAGIPP EIGLSETQQT LVLNGLRGQV RLQTDGQLKT
GRDIISMALL GADEYAFGTA ALIVLGCVMM RKCHTNLCPV GVATQNEKLR EHFRGHYQYL
INYFEFLAQE VREYLAAMGF TRLQDIIGRT DLIEIAPHSQ TGKIGGLDFS RILHQVDNGA
DIHYIKNRPL DLSEVKDRSI IAAAHEALDS KRPVELEYTI SNTDRSVGTM LAGEVATRYG
HEGLPDGTIS VKFKGSAGQS FGAFLTPGIS FRLEGEANDY VAKGLSGGRI AVLPPMGSCF
DASKNTIAGN TLMYGATSGE VYINGCVGER FAVRNSGAIA VVEGVGDHCC EYMTGGRVVV
LGHTGRNFAA GMSGGIAYVW DRERTFDYFC NMEMVELSLL EDSAARKELR ELIERHWKYT
GSKLARTLLD NWQQHVDEFI QVTPIEYKRV LAEEQMKKLQ QKIAEVQRDY
//
