ID E6W687_DESIS Unreviewed; 1481 AA.
AC E6W687;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ADU66123.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:ADU66123.1};
GN OrderedLocusNames=Selin_1388 {ECO:0000313|EMBL:ADU66123.1};
OS Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC Desulfurispirillum.
OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU66123.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU66123.1, ECO:0000313|Proteomes:UP000002572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC {ECO:0000313|Proteomes:UP000002572};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA Bini E., Woyke T.;
RT "Complete sequence of Desulfurispirillum indicum S5.";
RL Submitted (DEC-2010) 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; CP002432; ADU66123.1; -; Genomic_DNA.
DR RefSeq; WP_013506004.1; NC_014836.1.
DR STRING; 653733.Selin_1388; -.
DR MEROPS; C44.003; -.
DR KEGG; din:Selin_1388; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_0; -.
DR InParanoid; E6W687; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000002572; Chromosome.
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:ADU66123.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572}.
FT DOMAIN 16..404
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1481 AA; 163447 MW; E0E20ACA6847B077 CRC64;
MSELVTNLAE EFKDSCGFGI IANIRNTPSH QLLTDAVTAL SRMMHRGAIA ADGKTGDGSG
ILCAMPVQFM REQAQAMGIS LPAQFAVAVL FLTDEDQQKK VFEECCGRND LKVLGYRGVP
VNTEALGEHA ASMLPSIVHA FVVPDSLIAT KRMDALLYLS RRQMERHFAS DDHFHVASFS
RTVVSYKGLV MPLHLQTLYA DLSDPDFKIS FALFHQRFST NTLPKWKLAQ PFRMICHNGE
INSLRANAFN SLYKFNAARS RVFSRDELQS LLPVLQDGVS DSANLDNMFE FLIANGIDFF
KAIRSLIPPP RHNVANMPAK LRSFYEYTSG SFEPWDGPAA VGVTDGRYVG CVLDRNGLRP
AKYIVTRDGR FIITSEFGVL DIAPENIRER GRLQSGQMIA ADLKNGRIFY SDDIDEYLMN
SQPYSKWLTE NTYYLQEFMD RQFENHDDYR YENLVAMQRY HNVTHETVEL LVKPMLISGQ
EPTGSMGDDC PVAAFSDVQR NFTDFFRQKF AQVTNPPIDP IREKVVMSTT TGFGELYNVL
DETPDRAKRL KTISPILSRD ILDALLSFGD PDRPRFDPCY KYGFFGTAYH GVCLREALEN
LSQQVIAAVR DHGVRIVLLD DRGLDAQNRL IPMAMAVGYV NQQLVEANLR HRATLVACTG
EVFDSHSAAV MMAFGAMAIY PYLLYATTLS VLSSESRLSQ RDIRIALKHT FDAITKGILK
VMSKMGISAV SSYRNSALFD VIGLSREVVE NCFRGASILL PGLDYQDIEE RIEKVHGEVF
RRQHMQPIYP LPMGGFYKHH TGGEYHDYSP RAVQLLHGFA SSQKREDYIA FRDIIESRGL
KMIRDFFTLR PAGTPLPIEE VEDIKAICSR FDSAAMSLGA LSPEAHEALA EAMNILGGKS
NCGEGGEAAE RYKSVKNSKI KQIASGRFGV TPAYLRSAEE IQIKIAQGAK PGEGGQLPGE
KVTPLIASLR FTIPGVTLIS PPPHHDIYSI EDLAQLIFDM KQVNPDARVS VKLVSSAGVG
TIAAGVAKAY ADKIIISGSD GGTGAAQYAS IKFAGNPWEI GLTEAHNALK ANNLRQMVEL
QTDGGLKTGR DVVKAALMGA ESYGFGTSLL AILGCKLLRV CHLNRCSVGI ATQSDQLREH
YQGTVDKVVA YLTNVAEDVR EILASLGLRS LQEAVGRVDL LEVVDQPLAK KFDFSAVLRQ
IPGQNTVTAP SNPPFDHNEF EKGVLKEIAT VLRNPQQSIL VERTIQNVHR SFGAMISGEV
AKYYGDAGLD KDQILIHLKG IAGQSLGAFL IDGISINLNG VANDYVGKGM HGGKIIIVPT
NQWENYSAVG NTCLYGATGG KLFVCGTAGE RFAVRNSGAL AVVEGTGDHA CEYMTGGTVV
ILGDTGINFG AGMTGGAAFV YDRKNRFIDK LNQELVEAKR IDVDADNEGK LYLKKILFSY
YSHTRNARAK MILDNYREEL EYFWMVVPKD MKAPLNPKDG N
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