ID A0A1F2PL71_9FIRM Unreviewed; 1529 AA.
AC A0A1F2PL71;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ferredoxin-dependent glutamate synthase 1 {ECO:0000313|EMBL:OFV71604.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:OFV71604.1};
GN Name=gltB_1 {ECO:0000313|EMBL:OFV71604.1};
GN ORFNames=ACWI_09090 {ECO:0000313|EMBL:OFV71604.1};
OS Acetobacterium wieringae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52694 {ECO:0000313|EMBL:OFV71604.1, ECO:0000313|Proteomes:UP000176244};
RN [1] {ECO:0000313|EMBL:OFV71604.1, ECO:0000313|Proteomes:UP000176244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1911 {ECO:0000313|EMBL:OFV71604.1,
RC ECO:0000313|Proteomes:UP000176244};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Acetobacterium wieringae DSM 1911.";
RL Submitted (SEP-2015) 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:OFV71604.1}.
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DR EMBL; LKEU01000018; OFV71604.1; -; Genomic_DNA.
DR STRING; 52694.ACWI_09090; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000176244; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:OFV71604.1}.
FT DOMAIN 24..419
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1529 AA; 168351 MW; A687157AE6D6FDA1 CRC64;
MRMKHTSLPP KQGLYDPAFE HDACGIGAIV HIKGKKSHDI VKQALTTLVN LQHRGGRGSE
QNTGDGAGIL IQIPHQFMEK ASIKEGFTLP QPGDYGLGML FMPTDVNERN QCERILEDII
IEEGQTLLGW RDVPVDLCDL GKTAVDSMPF LKQVFIQKDA ALTDTMDFER KLYTIRKQAE
KKTKKAGLSF YAASFSSRTI VYKGMLTEDQ VGQFYLDLQD PDVTTAIAMV HSRFSTNTFP
SWERAHPNRY VIHNGEINTL RGNVNWMYAR QSLLQSELFG NELEKTFPVV DVDGSDSSIF
DNTFEFLSLT GRSLAHSAMM MIPEPWAKHQ TMSPEKKAFY NYHARMLEPW DGPAAIAFTD
GVRLGAVLDR NGLRPSRYYV TKDDMVILSS EVGVLDIPPE NILCKERLKP GRMLMIDTEK
GEIINDEDLK HAVASQQPYA EWLEKHNIPI TKLPEPKTKY VTDKATLIQR QKTFGYTYED
LKALIIPMAK DGVDPIGAMG NDIPLAVLSD KSQVLFNYFK QMFAQVTNPP IDALREELIT
GTEVYLGGEG NLINPLPESC HQISLDMPIL SNEDLEKIRE LNDPRIKTIT LSTLFESNTG
GDGLEKALND IFAAADQAIA DGNTIIVLSD RGVNEKMVPI PSALAIAGLH HHLVNNLTRT
RVSLVVESGE PREVHHFAVL IGYGATAVNP YLAFESVADL IDRGMLTDVA YEKAVKTYIK
TVSKGVIKVL SKMGISTILS YHGAQIFEAV GINSEVIDKY FTRTPSRIEG IGINEIARES
QMRHDEAYRN PFGDANALES GGNFQWRADG EYHTYNPEAV YKLQTACRNG DYQTYQEYTA
LINEQSQRTC TLRGMMTFKD LAPISIDEVE SVESICTRFK TGAMSYGSLS SEAHECLAIA
MNRIGGKSNT GEGGEDPERH IPLHNGDSRL SAIKQVASGR FGVTSHYLSS AQEIQIKMAQ
GAKPGEGGQL PGRKVYPWVA KTRYSTPGVG LISPPPHHDI YSIEDLAELI HDLKNANREA
SINVKLVSEV GVGTIAAGVA KAKADVILIS GYDGGTGASP RTSIRHAGLP WELGLAETHQ
TLVLNNLRTR VKVETDGKLL TGKDLAVATL LGAEEYGFAT APLVILGCVM MRVCHLDTCP
VGVATQNPEL RKRFTGDPGH VVNFMKFIAQ ELREIMAELG FRTIDEMVGR SDKLEMNKAI
DHWKTKGLDF SSILYQPAIP EGGGLYCQIK QNHNIEKSKD LTELLALCQP ALEKAEKVVI
NTTIKNVNRV VGTIVGNEVT KRYGEAGLPE DTITINLKGS SGQSLGAFMP KGMTIKLEGD
ANDYFGKGLS GGKMVIYPPK EATFVPEENI IVGNVAFYGA TEGEAFIRGA AGERFCVRNS
GVTAVVEAVG DHGCEYMTGG KVVILGKTGR NFAAGMSGGI AYVLDLDENF CESCNAEMVD
LVKITDAVEL AELKELIIKH HDYTNSSLAQ KILDDFDHYA KQFTKVLPRD YKRMLDAMER
VKALGLTGDE ALMAAFEENN RDLSRVSGN
//