ID A0A245ZKG7_9SPHN Unreviewed; 1504 AA.
AC A0A245ZKG7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glutamate synthase large chain {ECO:0000313|EMBL:OWK30224.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:OWK30224.1};
GN Name=gltB {ECO:0000313|EMBL:OWK30224.1};
GN ORFNames=SPDO_19070 {ECO:0000313|EMBL:OWK30224.1};
OS Sphingomonas dokdonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=344880 {ECO:0000313|EMBL:OWK30224.1, ECO:0000313|Proteomes:UP000197290};
RN [1] {ECO:0000313|EMBL:OWK30224.1, ECO:0000313|Proteomes:UP000197290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21029 {ECO:0000313|EMBL:OWK30224.1,
RC ECO:0000313|Proteomes:UP000197290};
RA Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Sphingomonas dokdonensis DSM 21029.";
RL Submitted (MAR-2017) 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 -!- 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:OWK30224.1}.
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DR EMBL; NBBI01000003; OWK30224.1; -; Genomic_DNA.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000197290; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) 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:OWK30224.1}.
FT DOMAIN 22..421
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1504 AA; 163469 MW; 5B80F01BB2B19B23 CRC64;
MDQRDYLATH GMYRPEFEGD ACGVGLVAAT DGKPSRRVVQ SAIDALKAVW HRGAVDADGK
TGDGAGLHVD LPLRFFDDAI AMSGHKVRPN RLAVGMVFLP RTDLAAQETC RTIVESAIIE
AGYTIYGWRQ VPVDVSVIGM KAQATRPEIE QIMIAGPMPD EVDAAEFEKT LYLVRRRIEK
RVIAAQIQGF YVCSLSCRSI IYKGLFLAES LSVFYPDLTD KRFESRVAIF HQRYSTNTFP
QWWLAQPFRC LAHNGEINTI RGNKNWMLSH EIRMASIAFG EHSEDIKPVI PAGASDTAAL
DATFEAICRS GRDAPTAKLM LVPEAWQSDV VDDMPPAHAA MYQYLASVME PWDGPAALAM
TDGRWAVAGM DRNALRPLRY TQTADGLLIV GSESGMVVVP ESTVVAKGRL GPGQMIAVDL
AEGKVYDDRA IKDRIAGEAD YAGMIGNFAT IDDLPPAPAT SVPHYDRAEL ARRQVAAGQT
LEDMELILAP MVETAKEAIG SMGDDTPLAV ISDKPRLISQ FFRQNFSQVT NPPIDPLRER
YVMSLKTRFG NLANILDTED RRERVLVLDS PVLTSTDWAR LKTYFASAAA EIDATFEANG
GADKLRAAIQ RIRNEAEQAV RQGKSEIFLT DEYVGPERIA IPGVLAAAAV HTHLVRRGLR
SYASINVRTA ECLDTHYYAV LIGVGATTVN AYLAEAAIAD RQARGLFGDV PLEECLKRHR
KAIEEGLLKI LSKMGIAVIS SYRGGYNFEA VGLSRALVND FFPGMPAKIS GEGYASLHIN
AKERHDAAFD EAVVNLPIGG FYRQRHTGEA HAFSAQLMHL LQTSVSTDSY STYLQFSRGV
GDLPPIYLRD LLQFNFPAEG VPVDQVEPIT EIRKRFVTPG MSLGALSPEA HETLAIAMNR
IGAKAVSGEG GEDKSRYQPY ENGDNANSVI KQIASGRFGV TAEYLNACEE IEIKVAQGAK
PGEGGQLPGF KVTEFIAKLR HATPGVTLIS PPPHHDIYSI EDLAQLIYDL KQINPRARVC
VKLVSSAGIG TVAAGVAKAH ADVILVSGNV GGTGASPQTS IKYAGTPWEM GLSEVNQVLT
LNGLRGRIKL RTDGGLRVGR DIVIAAILGA EEFGIGTLSL VAMGCIMVRQ CHSNTCPVGV
CTQDPRLREK FVGTPEKVIN LMTFIAEEVR DILARLGVRS LDEVIGRTEL LRQVSRGAEH
LDDLDLNPIL AKVDATDAER RFSLNTFRNE VPDSLDAQII KDAAAVFSRR EKMQLTYSVR
NTHRAVGTRL SSEITRTFGM SALNDHHVTI RLRGSAGQSL GAFLCKGITL EVFGDANDYV
GKGLSGGMIV VRPAVSSPLR SQENTIVGNT VLYGATSGAL FAAGQAGERF AVRNSGATVV
VEGCGANGCE YMTGGTAVVL GAVGQNFGAG MTGGMAFIYD CEDNFARRAN PENITWQRLA
SAHWSGVLRD LIERHVEATD SKWGRGILED WDRAAPRFWQ VVPREMLSRL VHPLDDAPAM
EAAE
//
