ID C4ZD50_AGARV Unreviewed; 1517 AA.
AC C4ZD50;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ACR76013.1};
GN OrderedLocusNames=EUBREC_2274 {ECO:0000313|EMBL:ACR76013.1};
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR76013.1, ECO:0000313|Proteomes:UP000001477};
RN [1] {ECO:0000313|EMBL:ACR76013.1, ECO:0000313|Proteomes:UP000001477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990 {ECO:0000313|Proteomes:UP000001477};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001107; ACR76013.1; -; Genomic_DNA.
DR RefSeq; WP_012743108.1; NC_012781.1.
DR STRING; 515619.EUBREC_2274; -.
DR MEROPS; C44.003; -.
DR PaxDb; 515619-EUBREC_2274; -.
DR KEGG; ere:EUBREC_2274; -.
DR HOGENOM; CLU_000422_8_2_9; -.
DR Proteomes; UP000001477; Chromosome.
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 25..416
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1517 AA; 168771 MW; 9966883358FAF2DB CRC64;
MSKQWNESTA TAKGLYDPRY EHDNCGIGAV VNIKGIKTHE TVENALKIVE NLKHRAGKDA
DGKTGDGVGI LLQISHKFFK KVTKPLGIEL GDERDYGVGM FFFPNDEFKT IQAKKMLEVI
VEKEGLEFLG WREVPTEPDK LSKKARDCMP CIMQCFVKRP EDVERGLEFD RKLYVARRVF
EQSNDNTYVV SFSSRTIVYK GMFLVEQLRQ FFMDLQDPDY ESAIATVHSR FSTNTNPSWE
RSHPNRFIVH NGEINTILGN SDKMSAREEN MESPKLKKEF QKVLPVINAA GSDSAMLDNA
LEFLVMSGME LPLAVMIMIP EPWANNSIMT QKKKDFYQYY ATMMEPWDGP ASIVFSDGDL
VGAVLDRNGL RPSRYYVTDD DYLILSSEVG VLEIDPTKIV KKDRLRPGKM LLVDTVAGKI
IDDDELKERY ADKQPYGEWI DRYMVNLKDL KIPNQRVPEY TKEERQRMQR AFGYTYESLK
DSILPMAKNG VEGTAAMGTD TPLAALSGNR EPLFNYFKQR FAQVTNPPID SIREEVVTST
TLYIGEAGNV LEEKPENCRV LKINNPILTN TDLMKIKNLK ADGFKVEVLP IIYYKNTSLE
KAVDRLYIEA DRAYRDGANI IILSDRGVDE NHVAIPSLLA VAALQQYLVK TKKRTSLSLI
LESGEPREVH HFATLLGFGA SAINPYLAQD TVKQLVDEHM LDKDYYAAID DYNHAIITGI
VKIAAKMGIS TIQSYQGSKI FEAIGIDKSV IDKYFTNTVS RIGGITLQDI ENDVNELHSA
AYDPLGLETD VTLDSKGRHK MRSGADDHLY NPATIHLLQQ STQRGDYNLF KQYTALVDEE
EKNTNIRGLM DFNYPKKGVK LEEVESVDSI VTRFKTGAMS YGSISKEAHE TLAIAMNYLH
GKSNTGEGGE DKDRLTIGKD GKNRCSAIKQ VASGRFGVTS RYLTSAQEIQ IKMAQGAKPG
EGGHLPGKKV YPWIAKTRLS TPGVALISPP PHHDIYSIED LEQLIFDLKN ANRDARISVK
LVSEAGVGTV AAGVAKAGAQ VVLISGYDGG TGAAPSSSIH NAGLPWELGL AETHQTLLMN
GLRNKVRIET DGKLMSGRDV AIAACLGAEE FGFATAPLVT MGCVMMRVCN LDTCPAGIAT
QNPELRKRFA GKPEYVENFM RFIAEELREY MAKLGVKTVD ELVGRGDLLK KRDNLSERQS
KIDLDCILNN PFDGKKQSVI FDPKQVYDFE LSKTKDMTEI MTQLKSALES GQKRAIEIEV
TNTNRSLGTI FGSEITKKYD DTLDEDTFVI KCNGAGGQSF GAFIPKGLTL ELVGDSNDYF
GKGLSGGKLI VYPPAGVKFE KDDNIIIGNV ALYGATSGKA FINGVAGERF CVRNSGATAV
VEGVGDHGCE YMTGGRVVIL GKTGKNFAAG MSGGIAYVLD EDNDLYMRTN KQMVFTEEVS
NKYDVLELKE MIKEHVTLTN SEKGKEILDH FSEYLPKFKK VIPYDYNRMQ MAIVQMEEKG
LNAEQAQIEA FYASTRG
//
