ID R7FA75_9FIRM Unreviewed; 1522 AA.
AC R7FA75;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:CDE11566.1};
GN ORFNames=BN611_00941 {ECO:0000313|EMBL:CDE11566.1};
OS Ruminococcus sp. CAG:330.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262954 {ECO:0000313|EMBL:CDE11566.1, ECO:0000313|Proteomes:UP000018377};
RN [1] {ECO:0000313|EMBL:CDE11566.1, ECO:0000313|Proteomes:UP000018377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:330 {ECO:0000313|Proteomes:UP000018377};
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:CDE11566.1}.
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DR EMBL; CBIH010000015; CDE11566.1; -; Genomic_DNA.
DR STRING; 1262954.BN611_00941; -.
DR Proteomes; UP000018377; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000018377}.
FT DOMAIN 25..417
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1522 AA; 168913 MW; 2BFB1ADBCC0D2112 CRC64;
MDNYRTQEPF AKNGLYDPRF EHENCGIGAV VNMSGKTDRK VVDSALRIVE TLEHRAGKDA
EGKTGDGVGI LLQISHTYFS KVAKEAGIKI GGKREYGIGM FFFPQTKEKY EEAMQTFEDV
LKEENLEFLG WREVPVNPDV LGTKALDSMP HIMQAFIKKP EDCAKGLEFD RKLYIARMVF
EKRNHETYVV SCSSRTIVYK GMFLVNQLRL FYHDLNSPDY HSAIGIVHSR FSTNTNPSWQ
RSHPNRMMVH NGEINTITGN VDKMLSRENI LHCDTLDARM KDILPMLDVR GSDSARLDNT
LEFMTMSGMD LPLAVMMTIP EPWQHIPTMS REKRAFYQYY ATMMEPWDGP ASIIFTDGDV
MGAVLDRNGL RPSRYYVTDD GYLILSSEVG ALDDIPVERI IKKERLHPGK MLLVDTVQGK
LIDDETIKNH YAKRQPYGEW LDHNLFELRE LKIPNKRPFR YSGKELLRLQ RAFGYGYESL
YHVMVPMALN GAEPTSAMGT DTPIPAMSKK NPPLFDYFKQ MFAQVTNPPI DSIRESVITD
TTVYLGVAGN ILKEEERNCR VLKVNNPILT NLDLMKIRGM NIEGLQTADI SMLYTKDVSL
HDAIEALYHQ AEKAHADGAT ILILTDRGVD KDHIAIPSLL AVAALETYLV RTRKNTAISI
IVETAEPCEV HHFATLLGFG ASAVNPYLAL DTLYDMINRG LVDKDYSQAS KAYIDAVVSG
IVKIASKMGI STIQSYQGSK IFEALGISDS VMQEYFPDTV SRVGGIDLDD IAARSLKMHN
SAFDPNELGM DEGLSSIGWH KERSNQEEHL YNPETIHLLQ QATWRDDYNL FKQYSACVNA
ENRHITLRST LDFQFAEDGG IPIEEVESVE CIMRRFKTGA MSYGSISQET HECMAIAMNR
IGGKSNSGEG GEDLERIVTA GSAVDKCSAI KQVASGRFGV TSKYLTSAKE IQIKMAQGAK
PGEGGHLPAK KVYPWIAKTR HSTPGVALIS PPPHHDIYSI EDLAQLIYDL KNANKKSRIS
VKLVSEAGVG TIAAGVAKAG AGVILISGYD GGTGAAPGSS IHNAGLPWEL GLSETHQTLI
QNNLRSKVVI ETDGKMMTGR DVVIAAMLGA EEYGFATAPL VTMGCVMMRV CNLDTCPVGV
ATQNPELRKR FHGKPEYVIN FMRFIAQEMR EYMAKLGIHT VDELVGRSDL LVQKHYPEGS
RESKIDMSRI LNNPYALPES HEKMHFVPED VFDFKLDQTI DETVIIPEMK EALAKKQKKR
IEINVSNLNR ALGTLFGAEI TRKYYNNLED DTFVIKCNGS GGQSFGAFIP KGLTLELEGD
SNDYFGKGLS GGKLAVYPPK GSKFQEDENI IIGNVALFGA TSGKAFINGV AGERFCVRNS
GASVVVEGVG EHGCEYMTGG CAVILGEVGK NFAAGMSGGI AYVLDNENDL YTKLNKALVG
FSGVTKPEDQ KQLHDLIEEH VAWTGSQLGK KILADFDAYL PHFKKIVPHD YAKMMETIAT
LQKDGMSLED AQIEAFYANT RN
//
