ID A0A158HZJ3_9BURK Unreviewed; 1567 AA.
AC A0A158HZJ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:SAL49409.1};
GN ORFNames=AWB64_05205 {ECO:0000313|EMBL:SAL49409.1};
OS Caballeronia sordidicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=196367 {ECO:0000313|EMBL:SAL49409.1, ECO:0000313|Proteomes:UP000054893};
RN [1] {ECO:0000313|EMBL:SAL49409.1, ECO:0000313|Proteomes:UP000054893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22029 {ECO:0000313|EMBL:SAL49409.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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 ---------------------------------------------------------------------------
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; FCOC02000022; SAL49409.1; -; Genomic_DNA.
DR RefSeq; WP_060858217.1; NZ_FCOC02000022.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000054893; 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}.
FT DOMAIN 28..428
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1567 AA; 170975 MW; 0813183AE58796C8 CRC64;
MNDQLPTTLG SAPAAQGMYD PENEHDSCGV GFVAHIKGKK RHEIIQQGLK ILENLDHRGA
VGADKLMGDG AGILIQIPDG FYREEMAKQG VTLPPEGEYG VGMIFLPKEH ASRLACEQEL
ERTVKAEGQV VLGWRDVPVD ASMPISPTVK ASEPLIRQIF IGRGKDIVVT DALERKLYVI
RKTASHRIQA LKLKHGKEYF VPSMSARTVV YKGLLLAGQV GVYYRDLQDE RTVSALALVH
QRFSTNTFPA WELAHPYRMI AHNGEINTVK GNVNWLNART GAIASYVLGD DLPKLWPLIY
PGQSDTASFD NCLELLVMAG YPLVHAMMMM IPEAWEQHTL MDDNRRAFYE YHAAMMEPWD
GPAAIAFTDG RQIGATLDRN GLRPARYVIT DDDLVILASE AGVLPVPESK IVKKWRLQPG
KMFLIDMEQG RIIDDKELKD NLANGKPYKS WIDAVRIKLD EIEPKAEEVD TQRREAAALL
DRQQAFGYTQ EDVKFLMAPM AQLGEEAVGS MGNDSPLAVM SNKNKTLYHY FKQLFAQVTN
PPIDPIRENM VMSLVSFVGP KPNLLDTTNI NPTMRLEVSQ PVLDFKDIAK IRAIDKYTGG
KFSSYELSIC YPVVWGNEGV EARLASLCAE AVDAVKSGYN MLIVSDRKMD RDNLAIPALL
ATSAIHTHLV QHGLRTSTGL VVETGSARET HHFALLAAYG AEAVHPYLAL ETLAQMAEGL
KGDLSADKAI YNYTKAVGKG LYKVMSKMGI STYMSYTGAQ IFEAVGLSSD LVEKYFKGTA
SKVGGIGIFE VAEEAIRLHR EAFGENPILA TMLDAGGEYA YRVRGEEHMW TPDAIAKLQH
SARSNSYQTY KEYAHLINDQ TKRHMTFRGL FEFKVDPTKA IPLDEVEPAK EIVKRFATGA
MSLGSISTEA HATLAVAMNR IGGKSNTGEG GEDANRYRNE LRGIPIKNGD TMRSVIGDEV
VTDIPLKDGD SLRSRIKQVA SGRFGVTAEY LSSADQIQIK MAQGAKPGEG GQLPGHKVSD
YIGKLRYSVP GVGLISPPPH HDIYSIEDLA QLIHDLKNVN SSSSVSVKLV SEVGVGTVAA
GVAKAKADHV VIAGHDGGTG ASPLSSLKHA GTPWELGLAE TQQTLVLNRL RGRIRVQADG
QMKTGRDVVI GALLGADEFG FATAPLVVQG CIMMRKCHLN TCPVGVATQD PVLRAKFTGQ
PEHVVNFFFF IAEEVREIMA QLGIRKFDDL IGHAELLDTK KGVEHWKAKG LDFSKVFYQV
PNDGSIATKH VETQDHGLEK ALDHVLIEKS KAAIEKGEHV SFIQPVRNVN RTVGAMLSGL
VARKHGHDGL ADDAIHIQLK GTAGQSFGAF LAKGITLDLV GDGNDYVGKG LSGGRIIIRP
TNDFRGKSEE NIICGNTVLY GAIEGEAYFR GVAGERFAVR NSGATAVVEG TGDHGCEYMT
GGTVVVLGET GRNFAAGMSG GVAFVYDPDG AFGSKCNKAM VALDPVLQQA EQERTVDRAL
WHTGQTDEAL LKGLIERHFQ TTGSPRAKAL LENWDASRRQ FVKVFPTEYK RALGELGAKK
AKDAIAA
//
