ID A5GIP6_SYNPW Unreviewed; 1532 AA. AC A5GIP6; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=glutamate synthase (ferredoxin) {ECO:0000256|ARBA:ARBA00039085}; DE EC=1.4.7.1 {ECO:0000256|ARBA:ARBA00039085}; GN Name=gltS {ECO:0000313|EMBL:CAK22811.1}; GN OrderedLocusNames=SynWH7803_0385 {ECO:0000313|EMBL:CAK22811.1}; OS Synechococcus sp. (strain WH7803). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=32051 {ECO:0000313|EMBL:CAK22811.1, ECO:0000313|Proteomes:UP000001566}; RN [1] {ECO:0000313|Proteomes:UP000001566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH7803 {ECO:0000313|Proteomes:UP000001566}; RG Genoscope; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. 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; L-glutamate biosynthesis via GLT CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin CC route): step 1/1. {ECO:0000256|ARBA:ARBA00037928}. CC -!- PATHWAY: Energy metabolism; nitrogen metabolism. CC {ECO:0000256|ARBA:ARBA00004802}. CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}. CC -!- SIMILARITY: Belongs to the glutamate synthase family. CC {ECO:0000256|ARBA:ARBA00009716}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CT971583; CAK22811.1; -; Genomic_DNA. DR STRING; 32051.SynWH7803_0385; -. DR MEROPS; C44.003; -. DR KEGG; syx:SynWH7803_0385; -. DR eggNOG; COG0067; Bacteria. DR eggNOG; COG0069; Bacteria. DR eggNOG; COG0070; Bacteria. DR HOGENOM; CLU_000422_8_2_3; -. DR OrthoDB; 9758182at2; -. DR Proteomes; UP000001566; 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:SF1; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE 1, CHLOROPLASTIC_MITOCHONDRIAL; 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:CAK22811.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001566}. FT DOMAIN 27..419 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000259|PROSITE:PS51278" SQ SEQUENCE 1532 AA; 163934 MW; 2CB9FA7B096D6BC5 CRC64; MSHPTGSLWP YSDSAAPEAV AGEKDACGVG FLAQLSGETS HWVLQQALRG LGCMEHRGGC GGDGDSGDGA GVLCQIPWTY LKAVWPEAAS ARGLGMMFMP QDPERRELAR RFCKEEAEAL GLTSAGWRVV PVDSSVLGPM ARDTAPVIEQ WSLAGGPDGD AFEALLLRLR RRIGARARQA WGFEGSRDLY VASLSSRTVV YKGMVRSEVL AQYYADLRDP RFEVSFAVYH RRFSTNTLPR WPLAQPMRLL GHNGEINTLL GNLNWAKASE ASLADVWGEA ANDLNPVVNP AFSDSANLDA TLELMVRSGR SITDSLITLV PEAFRNQPDL EDRPAVTAMY EFNAGIQEPW DGPALLVFAD GKRVGATLDR NGLRPARWCT TADGFVIMGS ETGVVDLSGK TVVQKGRLGP GQMVAVDLEN GQLLDNWTVK EDAAGRFPYG DWLQHHRRSV EAQPWTQDRQ IGELDLLRLQ TAMGFTAEDF DLVIEDMAGL GKEPTYCMGD DIPLAVLSDK PHLLYDYFKQ RFAQVTNPPI DPLREKLVMS LEMHLGERRP ALKPQAEAAA VIHLDTPVLN EAELAAISEQ GLPVATLSTH VAVEACAGGL SSALQRLCES AEEAVRGGAQ VLVLSDRVDG SGAAAQLTAT SVAMPALLAV GAVHHHLLRQ KLRLRCSLVI DTAQCWSTHH MACLIGYGAS AVCPWLTWET TRHWLAHPKT QKRIEQGKLP ALDADKVQAN VRVSLENGLR KILSKIGISL LASYHGAQIF EAIGLGADVI DTAFSGTTSR VAGMTLAELA NETLSLHAKA FPELNRSKLE FMGFVQYRTG GEYHLNSPDM AKALHAAVKT GPGYDHFSTY KTLLENRPVT ALRDLLEFKL APTPLPLDQV ESAESLCKRF CTGGMSLGAL SREAHEVLAV AMNRIGGKSN SGEGGEDPAR FQVLHDVDAE GRSQAFPSIG GLRNGDTACS AIKQIASGRF GVTAEYLRSG KQLEIKVAQG AKPGEGGQLP GPKVDDYIAW LRNSKPGVAL ISPPPHHDIY SIEDLAQLIH DLHQVHPKAP VSVKLVAEIG IGTIAAGVAK ANADVIQISG HDGGTGASPL SSIKHAGSPW ELGLTEVHRS LLENGLRDRV LLRADGGLKT GWDVVIAALL GAEEYGFGSV AMIAEGCIMA RVCHTNNCPV GVATQKEALR KRFTGVPEHV VNFFWYVAEE VRQLLSLLGV AKLEDLIGRS DLLQPRAVQL AKTQGVDLSS LLAPIQGSEE RSWLRHSAEA HGNGPILEDQ LLADAELMAA VESHGSLSRT IAIINTDRSV GARLAGEIAQ RHGNRGFKGQ LNLTFQGAAG QSFGAFLVQG MNVRLEGEAN DYVGKGMNSG RISLVPSDGC ANPGDQVILG NTCLYGATGG ELFAHGRAGE RFGVRNSGAR TVVEGAGDHC CEYMTGGVVV VLGSTGRNVG AGMTGGVTFL LDEGDRVTAR VNPEIVAVCS LTTSQQEETL KELLEAHVAA TGSSKASALL ADWAAAKGRF KVLIPPSERA AMGLVDQQAV AA //