ID A0A1H8AJK8_9SPHN Unreviewed; 1505 AA.
AC A0A1H8AJK8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glutamate synthase (NADPH) large subunit {ECO:0000313|EMBL:SEM69989.1};
GN ORFNames=SAMN05192583_0910 {ECO:0000313|EMBL:SEM69989.1};
OS Sphingomonas gellani.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1166340 {ECO:0000313|EMBL:SEM69989.1, ECO:0000313|Proteomes:UP000199206};
RN [1] {ECO:0000313|Proteomes:UP000199206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S6-262 {ECO:0000313|Proteomes:UP000199206};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FOCF01000002; SEM69989.1; -; Genomic_DNA.
DR STRING; 1166340.SAMN05192583_0910; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000199206; 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:UP000199206}.
FT DOMAIN 23..418
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1505 AA; 162710 MW; 3646A683FAC3320F CRC64;
MTDQRAYLAE HGMYRPDSEG DACGVGLVAS TDGTASRRVV QSAIDALKAV WHRGAVDADG
KTGDGAGIHV DLPLRFFDDA VAASGHRLLP NRLAVGMIFL PRTDLGAQET CRTIVESAII
EAGYTIYGWR QVPVDVSVIG LKAQATRPEI EQIMIAGPDP QTVDEAEFEK TLYLVRRRVE
KRVIAAQIHG FYICSLSCRS IVYKGLFLAE SLSAFYPDLQ DQRFESRVAI FHQRYSTNTF
PQWWLAQPFR CLAHNGEINT VRGNKNWMLS HEIRMASIAF GEHSEDIKPV IPAGASDTAA
LDAVFEAICR SGRDAPTAKL MLVPEAARAD MPANHAAMYN YLASVMEPWD GPAALAMTDG
RWAVAGVDRN ALRPLRYIRT SDGLLIVGSE AGMVPVPEST VVAKGRLGPG QMIAVDLAEG
VLLDDRAVKD RIAGEADYPA MTGAFHTLSD LPEMGDASVR FDRAELARRQ VAAGQTLEDM
ELILSPMVES AKEAIGSMGD DTPLAVISDK PRLISQFFRQ NFSQVTNPPI DSLRERHVMS
LKTRFGNLAN ILDTEDRREA VLVLDSPVLT GTHWARLRAH FGRSAAEIDC TFEAGGGPEK
LRAAIARIRQ EAEQAVREGR SELFLTDEHV SEDRVAIAGV LAAAAVHTHL VRRGLRSYAS
INVRSAECLD THYYAVLIGV GATTVNAYLA EAAIVDRQAR GLFGDLSLDE CLKRHRTAIE
EGLLKIIGKM GIAVISSYRG GYNFEAVGLS RSLVADLFPG MPAKISGEGY ASLHLSATIR
HDAAWDSAVA TLPVGGFYRQ RHTGETHAYS AQLMHLLQTA VSTDSYTSYL QFSRGVADLP
PVYLRDLLQF NFPGEGVPVD QVEAITEIRK RFVTPGMSLG ALSKEAHETL AIAMNRIGAK
AVSGEGGEDK ARYQPYENGD NANSTIKQVA SGRFGVTAEY LNACEEIEIK VAQGAKPGEG
GQLPGFKVTE FIARLRHATP GVTLISPPPH HDIYSIEDLA QLIYDLKQIN PRARVCVKLV
SSAGIGTVAA GVAKAHADVI LVSGHVGGTG ASPQTSIKYA GTPWEMGLSE VNQTLTLNGL
RGRIRLRADG GLKTGRDIVI AAILGAEEFG IGTLSLVAMG CIMVRQCHSN TCPVGICTQD
DRLRQKFVGT PEKVINLMTF IAEEVRDILA RLGCRSLDEV IGRTELLRQV SRGAEHLDDL
DLNPILAKVD ATDAERRFSL NTFRNEVPDS LDAQMIKDAA HVFSRGEKMQ LTYSVRNTHR
AVGTRLSSEI TRRFGMSTLA EGHVTVRLRG SAGQSLGAFL VRGVTLEVFG DANDYVGKGL
SGGTIVVRPA VSSPLKSQEN TILGNTVLYG ATSGRLFAAG QAGERFAVRN SGATVVVEGC
GANGCEYMTG GTAVVLGGVG ANFGAGMTGG MAFVYDPDGA FDRRANPDSI VWRRLSSRHW
EGLLHQLVCD HAAATDSRWS KGLRDDWDRV SGDFWQVVPK EMLTRLGHPL EDEPVSVAGD
LVAAE
//
