ID G4E5R7_9GAMM Unreviewed; 1538 AA.
AC G4E5R7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:EGZ45788.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:EGZ45788.1};
GN ORFNames=ThisiDRAFT_1646 {ECO:0000313|EMBL:EGZ45788.1};
OS Thiorhodospira sibirica ATCC 700588.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiorhodospira.
OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ45788.1};
RN [1] {ECO:0000313|EMBL:EGZ45788.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ45788.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL Submitted (SEP-2011) 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:EGZ45788.1}.
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DR EMBL; AGFD01000030; EGZ45788.1; -; Genomic_DNA.
DR RefSeq; WP_006787660.1; NZ_MU255056.1.
DR STRING; 765914.ThisiDRAFT_1646; -.
DR PATRIC; fig|765914.3.peg.1632; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR OrthoDB; 9758182at2; -.
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:EGZ45788.1}.
FT DOMAIN 22..415
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 904..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1538 AA; 168910 MW; 296F58F4C510669F CRC64;
MSLRALPPAQ GLYDPALEHD ACGVGFICHI KNQKSHAIVA QGLEILERLA HRGAVGADPK
AGDGAGILVQ IPDAFFRAVL DFTLPAVGHY GIGMVFLPQD GALRAQLEQT IARYIDEGGQ
RLLGWRDVPV DNRDLGVSVL PSEPVVRQVF IERGANCADQ DSFERKLFVI RKRMDNAIRE
LGQSAYYVCS MSSRTVNYKG MLLADQVGKY YLDLQDERFT SALALVHQRF STNTFPTWDL
AQPFRMVCHN GEINTLRGNV NWMAARRHTM RSEVLGDDLD SIWPLIPEGQ SDSACFDNAL
ELLVMGGYSL AHAMMILIPE AWSGNVLMDE QRRAFYEYHM ALMEPWDGPA AMAFTDGRQI
GATLDRNGLR PARYLVTNDD IVMMASEMGV LDIAQERIIK KWRLQPGKML LIDLEQGRII
DDQEIKTQLA QAKPYGEWLK KTQIRLEELP TSVGPMSPDD ATLLDMQQAF GYTQEDLKFL
LTPMVRDGAE AVGSMGADNP VSVLSSRSKH LSTYFKQNFA QVTNPPIDPI REELVMSLVC
IIGPRPNLLG IHDAGKHWRL ETAQPVLTNQ DLERIRHIEY SLAGTFRTRT LDMVYPASEG
AQGMEAALAQ LCQQAEQAVL DGYNILILSD RNTNYNHIPI PALLATAAVH HHLIRRGLRT
SSGIVVETGA ALEVHHFATL SGYGAEAINP YLAFDTIESL LPSLGASLSF EEAQKRYIKA
IGKGLLKVMS KMGISTLESY CGAQIFDAVG LHSTFIEKYF TGTHGRIEGI GLSEVAREAV
RLHTQAYGGE HIYRRQLDVG GDYAFRIRGE DHVWTPDTIA KLQHATRAND AKTYEEYAHR
INEQNERLLT LRGLMDFDFA PTPIPLEEVE PASEIVKRFA TGAMSFGSIS YEAHSNLAKA
MNALGGKSNT GEGGEEPERF TPLPDGRANP ERSAIKQVAS GRFGVTTEYL VNGDEIQIKI
AQGAKPGEGG QLPGHKVNAQ IARVRHSTPG VGLISPPPHH DIYSIEDLAQ LIHDLKNVNP
EARISVKLVS EIGVGTVAAG VSKAHADHVT ISGYEGGTGA SPLTSIKHAG SPWEIGLAET
HQTLVLNRLR GRIVVQTDGG LRTGRDVVIG ALLGADEFGF ATAPLIVSGC IMMRKCHLNT
CPVGVATQDP ELRKRFTGQP EHVINYFFFV AEEVRQLMAK LGFRTFKEMI GQSDRLQMRR
AIEHWKAQGL DFSRLLQKPQ MPAEVAVHHC EQQQHGLEHA LDHTLIAQAE AALLRGEPVR
INTTVKNYNR TVGAMLSGRV AQRYGHAGLP DDTIYIKAQG IGGQSFGAWL ARGVTVELEG
EANDYVGKGL SGGRIVIYPP KQAAIARAED NIIVGNTVLY GAINGECYFR GVAGERFAVR
NSGAYAVVEG LGDHGCEYMT GGIVVCLGQT GRNFAAGMSG GIAYVYDEDG DFSQRCNQAM
VELLPISAAE DSEGVDEAAI LGDATRYDAA RLQLLIRRHL HYTDSALARH LLENWAQSLP
RFVKIMPVDY RNALEQIKAK QSRPPHVNKP LKGIAVYG
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