ID   A6UD11_SINMW            Unreviewed;      1574 AA.
AC   A6UD11;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ABR61541.1};
DE            EC=1.4.7.1 {ECO:0000313|EMBL:ABR61541.1};
GN   OrderedLocusNames=Smed_2711 {ECO:0000313|EMBL:ABR61541.1};
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR61541.1, ECO:0000313|Proteomes:UP000001108};
RN   [1] {ECO:0000313|Proteomes:UP000001108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR61541.1, ECO:0000313|Proteomes:UP000001108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419 {ECO:0000313|EMBL:ABR61541.1,
RC   ECO:0000313|Proteomes:UP000001108};
RX   PubMed=21304680; DOI=10.4056/sigs.43526;
RA   Reeve W., Chain P., O'Hara G., Ardley J., Nandesena K., Brau L., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Hauser L., Chang Y.J., Ivanova N., Mavromatis K., Markowitz V.,
RA   Kyrpides N., Gollagher M., Yates R., Dilworth M., Howieson J.;
RT   "Complete genome sequence of the Medicago microsymbiont Ensifer
RT   (Sinorhizobium) medicae strain WSM419.";
RL   Stand. Genomic Sci. 2:77-86(2010).
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; CP000738; ABR61541.1; -; Genomic_DNA.
DR   RefSeq; WP_012066927.1; NC_009636.1.
DR   RefSeq; YP_001328376.1; NC_009636.1.
DR   STRING; 366394.Smed_2711; -.
DR   MEROPS; C44.003; -.
DR   GeneID; 61611758; -.
DR   KEGG; smd:Smed_2711; -.
DR   PATRIC; fig|366394.8.peg.5912; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_5; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000001108; 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:ABR61541.1}.
FT   DOMAIN          47..448
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          944..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1574 AA;  172570 MW;  34EE0451C58BE495 CRC64;
     MTGHSPSRQI GLNLAQDAAT VVKTPAFSSG LPRKQGLYDP RNEHDACGVG FVAHLKGEKS
     HQIVRDGLFM LENLTHRGAV GADPLMGDGA GILVQIPDRF FREEMAKQGV TLPKAGEYAV
     GYLFMPRDEK LIAHFKDVIS EVVAEEGQIL LGYRDVPVDN SSLSKAPDIA ATEPHHVQVF
     IGAGREAATK DEFERRLFTL RKVISNRIYA EADGDDLGFY IVSLSTSTIV YKGMFLAYQV
     GAYYKDLADE RFQSAVALVH QRFSTNTFPS WKLAHPYRMV AHNGEINTLR GNVNWMAARQ
     ASVSSPLFGD DISKLWPISY EGQSDTACFD NALEFLVRGG YSLSHAVMML IPEAWAGNQL
     MSQERKAFYE YHAALMEPWD GPAAVAFTDG RQIGATLDRN GLRPARYIVT SDDRVIMASE
     AGVLPVAEEK IVKKWRLQPG KMLLIDMEEG RIISDEEVKS SLAGKHPYRH WLDNTQLILE
     ELKPVEPRAL RRDVSLIDRQ QAFGYTHEDT KLLMSPMATT GQEAIGSMGT DTPISAMSDK
     PKLLYTYFKQ NFAQVTNPPI DPIREELVMS LVSFIGPRPN ILDHEGMAHA KRLEVRQPIL
     TNGDLEKIRS IGHTEERFDT KTLDFTYDIT RGAEGMPEML DRLCERAEAA VKGGYNIIVL
     SDRQIGPDRV AIPALLATAA VHHHLIRKGL RTSVGLVVES GEPREIHHFC LLAGYGAEAI
     NPYLAFDTLV DMHKRGEFPK EVDEKEVVYR YIKAVGKGIL KVMSKMGIST YQSYCGAQIF
     DAVGLSSELV DKYFFGTATT IEGIGLEEIA AETVARHKAA FGSDPVLANT LDIGGEYAYR
     MRGESHAWTP DAIASLQHAV RGNAEDRYRE FSAMMNEQAS RMNTIRGLFT IRDAEAAGRK
     PIPVEEVEPA SEIVKRFSTG AMSFGSISRE AHTTLAIAMN RIGGKSNTGE GGEESDRYLP
     LPDGSTNPER SAIKQIASGR FGVTTEYLVN ADMLQIKVAQ GAKPGEGGQL PGHKVDATVA
     KTRHSTPGVG LISPPPHHDI YSIEDLAQLI YDLKNVNPEA DVSVKLVSEV GVGTVAAGVA
     KARADHITIA GFDGGTGASP LTSLKHAGSP WEIGLAETQQ TLVLNGLRSR IALQVDGGLK
     TGRDVVIGAL LGADEFGFAT APLIAAGCIM MRKCHLNTCP VGVATQDPVL RKRFKGTPEH
     VVNYFFFVAE EVRELLASLG ARKLDEIIGA SDLLERDRMI EHWKASGLDF SKIFHKVEAP
     KEATYWTERQ NHPIQDILDR KLIEKAKLAL ETKVPVAFEA EIKNVDRSAG AMLSGALAKR
     WGHKGLKDDT IHVTLKGTAG QSFGAFLARG ITFDLVGDGN DYVGKGLSGG RIVVRPPQNA
     RIVPHQSIIV GNTVLYGAIS GECYFNGVAG ERFAVRNSGA IAVVEGVGDH GCEYMTGGVV
     VVLGGTGRNF AAGMSGGVAY VLDEEGDFAR RCNMAMVELQ PVPEEDDMLE KLHHHGGDLM
     HKGMVDVSGD MTRHDEERLY QLISNHLHHT GSARAKEILD HWTDYRPKFR KVMPVEYRRA
     LEDMERMKMA EAAE
//