ID A0A1I0G7S0_9FIRM Unreviewed; 1546 AA.
AC A0A1I0G7S0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:SET66955.1};
GN ORFNames=SAMN04487771_103122 {ECO:0000313|EMBL:SET66955.1};
OS [Clostridium] aminophilum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1526 {ECO:0000313|EMBL:SET66955.1, ECO:0000313|Proteomes:UP000199820};
RN [1] {ECO:0000313|EMBL:SET66955.1, ECO:0000313|Proteomes:UP000199820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1P1 {ECO:0000313|EMBL:SET66955.1,
RC ECO:0000313|Proteomes:UP000199820};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOIL01000031; SET66955.1; -; Genomic_DNA.
DR STRING; 1526.SAMN02910262_02538; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000199820; 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:UP000199820}.
FT DOMAIN 48..439
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1546 AA; 171336 MW; 2FB5B21700BE073D CRC64;
MDNNTKGNQK ADEADQNCYV VPEAYRGHNK LWCPVTDGHP EDLGHDACGI GTVVNIDGHQ
DTKVLDDALS IVEKLEHRAG KDATGKVGDG VGILLQICHD FFSKVTKKAG ITVGEAGDYG
VGMFFLPENE KKRRFAKRMF EVIANKNGLQ VLGWRPVPSH PEILGKVALD CMPAIEQCFI
DRPDIYERGI DFDRRLYVLR REFEQSTEDT YICSLSSRTI VYKGMFLVGQ LRAFYDDLRD
ADNKTAIAIV HSRFSTNTTP SWDRAHPYRL LAHNGEINTI RGNIDRMLAR EETMQSPFLE
KEVEKIFPVV QTNGSDSSML DNTLEFLYMN GMELPLAMTV TIPEPWKHDR FMDSKKKDFY
HYYATMMEPW DGPAAIIFSD GDVVGATLDR NGLRPSRYYI TDDNRLILAS EVGVLDIDPK
HIVEKSRLQP GRMLLVDTRE QRIISDAEIK KHYAEKAPYG EWLDSNLVHL EKIKIPNHKL
ETHSPEMREK LYKVFGYTYD DVKEIILPMA QNGVEATSCM GHDTPLAVFD RKYQPLFYYF
KQLFAQVTNP PIDSLREKVV TDTTVYLGSD GNLLQDKAEN CRVLEISNPI LTGVELLKIR
ELDEPGFKAA VISLLYYQTT SLEKALQQLN ISVDRVCQRG ANIIILSDRG VDENHVAIPS
LLAVSSVEQH LVLTRKRTAV SLILESAEPR DVHQFATILG FGARAIYPYL AHECIAEIIE
AGILDKDTHT AIEDYNKAVM GGIVKIAAKM GISTIQSYQS AKIFEAIGLS QEFVDKYFTG
IVSRVGGIGI EDVAESVTWR HELAFDPMGE NVDAPDAACF SSRNFFRGKD TAEHLYNPKT
IMTMQKAVQK GDYKKFKEYT AMVDESPVPH TLRGIMKFVP KQKPVPISEV EPVESIVRRF
KTGAMSYGAI SLEAHEAMAI AMNRLGGKSN SGEGGEDPER FGTERNSAIK QVASGRFGVT
SPYLNSASEI QIKMAQGAKP GEGGHLPGKK VYPWIAKTRF STPGVSLISP PPHHDIYSIE
DLAQLIYDLK NANRRARISV KLASENGVGT IACGVAKAGA QVIHICGYDG GTGAAPMTSI
HHAGLPWELG ITEAHQTLIR NGLRNRVMIE TDGKLMTGRD VVIAALLGAE EYGFATTALV
SLGCMMIRAC NKDTCPFGVA TQNEKLRAKF KGKPEYVMNF MKFIAEEMRE IMAELGFRTV
QEMVGRTDCL GISEERASIT KRASKVDLSK ILDPEFAGLP ENVRHFDPEH VYDFHLEKTV
DEATLLPKFK SAMEKREHHE EKVKVSSTNR TFGTILGSEI TDRFGMGEKG SDLADDTFVV
HAFGGGGQSF GAFIPKGLTI RLHGDANDGF GKGLSGGKLV VTPPKDSAFR ASENIIIGNV
ALYGATGGKC YVEGIAGERF CVRNSGATAV AEGCGDHGLE YMTGGRAVIL GPTGKNFAAG
MSGGVAYVLD MDHTLYLKLN KDMVHFQAVT ERADIKELKD ILKDYVQETA SGLGKEILDN
IDRYLPSFKK IVPNDYQKVL EAVNHFEDNG SSQDDAEMEA FRMLFS
//
