ID B2JI14_PARP8 Unreviewed; 1567 AA.
AC B2JI14;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ACC71960.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:ACC71960.1};
GN OrderedLocusNames=Bphy_2788 {ECO:0000313|EMBL:ACC71960.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC71960.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC71960.1; -; Genomic_DNA.
DR RefSeq; WP_012402157.1; NZ_CADFGH010000028.1.
DR STRING; 391038.Bphy_2788; -.
DR MEROPS; C44.003; -.
DR KEGG; bph:Bphy_2788; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_4; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000001192; Chromosome 1.
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:ACC71960.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT DOMAIN 27..427
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1567 AA; 170885 MW; 17FAB4EC3CDC433F CRC64;
MNDHQQPIST VPAAQGLYDP QNEHDACGVG FVAHIKGKKS HEIIQQGLKI LENLDHRGAV
GADPLMGDGA GILIQIPDAF YREEMAKQGV TLPPAGEYGV GMIFLPKEHA SRLACEQELE
RTVKAEGQVV LGWRDVPVDH NMPISPTVKA SEPLIRQIFI GRGKDIMVTD ALERKLYVIR
KTASHRIQAL KLKHGKEYFV PSCSARTVVY KGLLLAGQVG VYYRDLQDER VVSALALVHQ
RFSTNTFPAW ELAHPYRMIA HNGEINTVKG NVNWLNARTG AIASHVLGDD LPKLWPLIYP
GQSDTASFDN CLELLVMAGY PLVHAVMMMI PEAWEQHTLM DDNRRAFYEY HAAMMEPWDG
PAAIAFTDGR QIGATLDRNG LRPARYIITD DDLVIMASEA GTLPIPESKI VKKWRLQPGK
MFLIDMEHGR IIDDKELKDN LANAKPYKSW IDAVTIKLDE IELNAGDVAT ERREAAALLD
RQQAFGYTQE DVKFLMAPMA QAGEEAVGSM GNDSPLAVMS NKNKTLYHYF KQLFAQVTNP
PIDPIRENMV MSLVSFVGPK PNLLDTNNIN PPMRLEVSQP VLDFKDIAKI RAIDQYTGGK
FSSYELNICY PAAWGKEGIE ARLASLCAEA VDAVKSGYNM LIVSDRKTDR DNVAIPALLA
TSAIHTHLVQ QGLRTSTGLV VETGSARETH HFALLAGYGA EAVHPYLAME TLAQMAAGMK
GDLSAEKAVY NFTKAVGKGL HKVMSKMGIS TYMSYTGAQI FEAVGLAEEL VNKYFKGTAS
KVGGIGLFEV AEEAIRLHRD AFGDNPVLAN MLDAGGEYAY RVRGEDHMWT PDAIAKLQHS
ARSNSYQTYK EYAHLINDQT KRHMTFRGLF EFKVDPSKAI PLDEVESAKE IVKRFATGAM
SLGSISTEAH ATLAVAMNRI GGKSNTGEGG EDENRYRNEL RGIPIKNGDT MKSIIGDEIV
TDIPLKEGDS LRSKIKQVAS GRFGVTAEYL ASADQIQIKM AQGAKPGEGG QLPGHKVSEY
IGKLRYSVPG VGLISPPPHH DIYSIEDLAQ LIHDLKNVNP SSSISVKLVS EVGVGTVAAG
VAKAKADHVV IAGHDGGTGA SPLSSVKHAG TPWELGLAET QQTLVLNQLR GRIRVQADGQ
MKTGRDVVIG ALLGADEFGF ATAPLVVEGC IMMRKCHLNT CPVGVATQDP VLRAKFQGQP
EHVVNFFFFI AEEVREIMAQ LGVRKFDDLI GHSEYLDMKK GIEHWKAKGL DFSRVFYQPS
VPASVARLHV ESQDHGLDRA LDHTLIEKAK AALEKGEHVS FIQPVRNVNR TVGAMLSGAV
AKKYGHDGLP DDAIHIQLKG TAGQSFGAFL AKGITLDLVG DGNDYVGKGL SGGRIIIRPT
NDFRGKSEEN IICGNTVMYG AIEGESFFRG VAGERFCVRN SGATAVVEGT GDHGCEYMTG
GTVVVLGETG RNFAAGMSGG VAYVLDVDGA FAAKCNKSMV ALDPVLQQAE QERTVDKALW
HQGETDEALL KGLIERHFQF TGSPRAKALL ENWDASRRQF VKVFPTEYKR ALGEMGAKKA
AKEVLAA
//
