ID C5D5U7_GEOSW Unreviewed; 1505 AA.
AC C5D5U7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ACS23395.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:ACS23395.1};
GN OrderedLocusNames=GWCH70_0484 {ECO:0000313|EMBL:ACS23395.1};
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS23395.1};
RN [1] {ECO:0000313|EMBL:ACS23395.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS23395.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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; CP001638; ACS23395.1; -; Genomic_DNA.
DR STRING; 471223.GWCH70_0484; -.
DR KEGG; gwc:GWCH70_0484; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_9; -.
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; cd02808; GltS_FMN; 1.
DR CDD; cd00504; GXGXG; 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:ACS23395.1}.
FT DOMAIN 37..406
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1505 AA; 165739 MW; 484F88142F98DD6A CRC64;
MNGEKQERSR FGAAYVMRQR WNPNHFKNFH QVEHDACGIV AAIEKQRIPT RENIMTCIDA
LVKMNHRAGF INGEGDGVGI HMDIPRKLWM EKLANVGQNP EIANDESFTV GHLFIDRSAD
VDHIKTKIKQ LFKKTGFLLI FESDRVTSSS ALGPIALRQE PVFWQVALLP SDNAQLTKRL
FDLMIEIEKD ENVHVASLNN FHVVYKVMGA GDILPKYYHD LAHPFIASTM TLGHNRYSTN
TLSNFFRVQP FSVLAHNGEI NTIAKLRDEA VMIGVPLTND GSDSQDLSRT LETLICRYDY
SLFEAMDILF PPIVNEIKAY PEHLQDLYTY IRESWGHFAQ GPAAIISRYE DEAVFSVDAL
GLRPLWKLET EKRFVFASEP GIIPASEYTG EPKPLAPGEK IGLTWFGGVI QVLEYEQFQE
EVYARFSKRF DITNFRKRLD VPKLENHVFT FVPTKVHNGQ YAAFGWDREH IQLLEQMAEK
GAEPIRSLGH DAPLAAINPN RKNLADFIKE SVAVVTNPAI DRDREMEHFS TRTVIGKRPF
LVDKTETSYV IELSSPILIE GKIGNDCATE LHHPSYDQIV HSFREKQLAH ILSATFTAEE
TIPQALERLS NEACEAVRSG KTLLVIDDAE AHQNGNLWID PLLITSAIDQ SLTKQDLRRD
CSILLRSGAI RSLHDFVVAY GLGANAISPY LMFATVASEE STAPVANLFK ALNKGLEKVI
STIGIHELRG YSRLFSSIGL HDEIADVLNI VNFFGSDSLK YDFEALKQDA IARAEDYANE
NAKPGKTFHL FPRIWKAIGE VAQTGSYDNY REKMNELETE TPTTIRHLLD IKKTEKQVPV
EKVDISVGEH SLPFVIASMS FGSQNEVAFR AYAEAADRLN MVSLNGEGGE IKDMLGKYPR
TRGQQIASGR FGVNAELLNS SNLLEIKIGQ GAKPGEGGHL PGSKVTAKIA EARNATIGSD
LISPSNNHDI YSIEDLAQMI AELKTANDKA KVAVKVPVVP NIGTIAVGIA KAGADIITLS
GFDGGTGAAR IHALQHVGLP VEIGVKAAHN ALLEAGLRNK VEIWADGGIK SALDVLKVML
LGANRIGFGT LSMIAIGCTT CRGCHLDTCH VGIATQIESV AQAKEHGLRR FVPRQFETAV
QGLVNLFTSF GNELKALTAS LGFTRLQDIV GRSDLLEQTR GLEQLNLSNL LEVLEVEQMA
QKEAAASAEE PSLLVAAGAE YLDYHVEDLH RSREFTNVTS EQRVLGSRVS CHRVRGRLDG
SYKKLPDVTL RYKNGSIPGN GLGAYNTHGI HIHVDGGGQD GVGKTAFGGS IFILKAKGKD
GKFYNGSVGK GFGYGAQKGL LIAQGNADAR AGIRLSGADM IIGGQVTTPI PEKEHGNIGT
RANIKGFAFE YMTNGRGIVL GDPGPWICAG MTGGVVYLRH QPEMGLTKAA LERRIAKGAQ
VRLEPLNERG KSDVQELLSK YIELLKEHGQ HEEAQSLQPL LEKPENHFFQ VIPTKEQADP
SVSTE
//
