ID F3KS59_9BURK Unreviewed; 1576 AA.
AC F3KS59;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:EGI77419.1};
GN ORFNames=HGR_06441 {ECO:0000313|EMBL:EGI77419.1};
OS Hylemonella gracilis ATCC 19624.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hylemonella.
OX NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI77419.1, ECO:0000313|Proteomes:UP000016368};
RN [1] {ECO:0000313|EMBL:EGI77419.1, ECO:0000313|Proteomes:UP000016368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI77419.1,
RC ECO:0000313|Proteomes:UP000016368};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
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:EGI77419.1}.
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DR EMBL; AEGR01000048; EGI77419.1; -; Genomic_DNA.
DR STRING; 887062.HGR_06441; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR Proteomes; UP000016368; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000016368}.
FT DOMAIN 30..430
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1555..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 171576 MW; A53295DF132D5B05 CRC64;
MKDGAMSAVA EIQHLEETGL YSGANEHDAC GVGFVAHIKG VKTHDIVRGA LKILENLDHR
GAVGADKLMG DGAGILIQLP DALYREEMAK QGVELPPPGE YGVGMIFLPK EHASRLACEQ
ELERAIRAEG QVLLGWRDVP VDRDMPMSPT VRTKEPIMRQ VFIGRGADVI VQDALERKLY
VIRKTASAAI QALQLKHSKE YYVPSMSSRT VVYKGLLLAN QVGEYFLDLK DSRCVSALGL
VHQRFSTNTF PEWPLAHPYR YVAHNGEINT VKGNYNWMKA REGVMSSPVL AADLKKLYPI
SFANQSDTAT FDNCLELLTM AGYPLSQAVM MMIPEPWEQH ATMDERRKAF YEYHAAMMEP
WDGPASIVFT DGRQIGATLD RNGLRPSRYC ITEDDLVIMA SEAGVLPVPE SQIVRKWRLQ
PGRMFLIDLE QGRMIEDEEL KANLAHSKPY KQWIENLRVK LDDVESSGSD GIPAAAANDL
LDRQQAFGMT QEDIKFLMAP MATNGEEGIG SMGNDSPLAV LSDKNKPLFN YFKQLFAQVT
NPPIDPIREA IVMSLVSFIG PKPNLLDINQ VNPPMRLEVS QPILDFADMA KLRRIETATQ
GKFRTATLDI TYPLSWGHEG VEAKLASLCA EAVDAIKGGK NILIISDRTS SSRQVAIPAL
LALSAIHQHL VREGLRTSAG LVVETGAARE VHHFAVLAGY GAEAVHPYLA METIAAMHKE
LPGDLSADKA IYNYVKAIGK GLSKIMSKMG VSTYMSYCGA QLFEAIGINS ATVAKYFTGT
PSRVEGIGVF EMAEEAIRMH KAAYSNDPVL ATMLDAGGEY AWRTRGEEHM WTPDAIAKLQ
HSTRANNFST YKEYAQLIND QSKRHMTLRG LFEFKIDPAK AIPVEEVEPA SEIVKRFATG
AMSLGSISTE AHATLAVAMN RIGGKSNTGE GGEDPARYRN ELKGIPIKKG ETLKSVIGES
RVEVDLPLQD GDSLRSKIKQ VASGRFGVTA EYLSSADQIQ IKMAQGAKPG EGGQLPGGKV
TEYIGFLRHS VPGVGLISPP PHHDIYSIED LAQLIHDLKN VAPHASISTK LVSEIGVGTI
AAGVAKCKSD HVVIAGHDGG TGASPWSSIK HAGSPWEIGL AETQQTLVLN RLRGRIRVQA
DGQMKTGRDV AIGALLGADE FGFATAPLVV EGCIMMRKCH LNTCPVGVAT QDPVLRKKFS
GKPEHVVNYF FFVAEEVRQI MAQLGIRKFD DMVGRADLLD TKQGIAHWKA KGLDFSRLFA
LPSAPADVPR RHVEEQEHGL EKSLDNVLIE KSRAAIDKGQ KVQFIEAARN VNRTVGAMLS
GAVTKVHPQG LPDNTIHIQL EGTGGQSFGA FLAKGITLYL IGEANDYTGK GLSGGRVVVR
PSIDFRGDAT RNTIVGNTVL YGATTGEAFF SGVAGERFAV RLSGATAVVE GAGDHGCEYM
TGGTVVVLGK TGRNFAAGMS GGVAYVYDED GKFAERCNTS MVSMEKVVLT AEQAGEAVNW
HRGLSDEAQL KKLLEDHNRW TGSKRARELL DHWKDARGKF VKVFPNEYKR TLAERKPGAA
EAPAKSASKK EVAAAK
//
