ID A0A1I0ZP65_9CELL Unreviewed; 1518 AA.
AC A0A1I0ZP65;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glutamate synthase (NADPH/NADH) large chain {ECO:0000313|EMBL:SFB27281.1};
GN ORFNames=SAMN05421867_11221 {ECO:0000313|EMBL:SFB27281.1};
OS Cellulomonas marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=988821 {ECO:0000313|EMBL:SFB27281.1, ECO:0000313|Proteomes:UP000199012};
RN [1] {ECO:0000313|EMBL:SFB27281.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6945 {ECO:0000313|EMBL:SFB27281.1};
RA de Groot N.N.;
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}.
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DR EMBL; FOKA01000012; SFB27281.1; -; Genomic_DNA.
DR STRING; 988821.SAMN05421867_11221; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000199012; 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; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
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:UP000199012}.
FT DOMAIN 28..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 904..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1518 AA; 163146 MW; FABDABB481EE1354 CRC64;
MSTTPASPPG LVPGAQGLYD PAAEHDACGF AFVATLRGTP GRDIVDAGLT ALLNLDHRGA
VGAEIDSGDG AGILTQIPDA FLRDVVDAEL PPVGQYAIGM AFLPADEAAR AEACRRIDAI
AAEEKLDVLA WRDVQVTADL VGPTARASMP AFRQLVVADP SRALAGLDLD RRAFRLRRRA
EREAGVYFAS LSSRTLTYKG MLTTAQLEPF FADLSDPRYA SELALVHSRF STNTFPSWPL
AQPMRLIAHN GEINTVRGNR NWVAAREGRL ASEALGDLAP LLPVCTPGGS DSGSFDEVLE
LLHLAGRSLP HAILMMVPEA WENHATMDPA RRAFYEYHST LMEPWDGPAA LTFTDGTLIG
SLQDRNGLRP GRFWVTEDGL VVCASEAGVL DLDPATIVHK GRLEPGRMFL VDTGTGRIVA
DDEVKGQLAA QKPYAQWVQE NSVFLEQLPE REHVAHSAAS VRRRQRAFGY TEEELKVILG
PMGATGAEPL GAMGSDTPVA VLSSRPRLLF DYFTQMFAQV TNPPLDAIRE ELVTSIGGAI
GPEPNLLADG PEHARKLVLP FPVLDNDQLA KIVHVQREPR YDFRSTIVRG LYKASGGGEA
LEARLEEIFA EVDAAIADGV SFLVLSDRNS DAELAPIPSL LLLSAVHHHT LRRHTRTQVS
LVVEAGDVRE VHHVALLVGY GAAAVNPYLA METVEDMARS GYLQVEPEKA VANLIKGLGK
GVLKVMSKMG ISTIASYRGA QVFEAIGLSQ PFVDKYFTGT TSRLGGIGLD VVAAEVAARH
ADAYPASGNR QAHQRLASGG EYQWRRDGED HLFDPETVFR LQHATRSRQY DVFREYTDRV
DGQSERLMTL RGLLQLREGV LPPVPVEEVE PVSEIVKRFQ TGAMSYGSIS AEAHETLAIA
MNRLGGRSNT GEGGEESERL HDPERRSAIK QVASGRFGVT SEYLTFADDI QIKLAQGAKP
GEGGQLPGHK VYPWIARTRH STPGVGLISP PPHHDIYSIE DLKQLIHDVK NANPSARVHV
KLVSEFGVGT VAAGVAKAHA DVVLIAGHDG GTGASPLTSL KHAGTPWEIG LAETQQTLVL
NDLRDRVSVQ VDGQLKTGRD VVIGALLGAE EFGFATAPLV VSGCVMMRVC HLDTCPVGVA
TQNPELRARF TGKPEFVVTF FEFLAQQVRE YLAALGLRSV QEAVGRVDLL DARQAVDHWK
AAGLDLSPVL AAPEPAEGST LHRSRSQDHG LERALDQQLI RLSADALERG EPVRIDLPVR
NVNRTVGTML GHEVTRRHGG DGLPPGTIDI TLTGSAGQSF GAFLPRGITL RLQGDANDYV
GKGLSGGRIV VRPDRSAQLA PHRNVVAGNV IGYGATSGEV LLSGLAGERF AVRNSGATLV
VEGVGDHGLE YMTGGTVLVL GPTGRNLGAG MSGGTAYVLD LVHGQLNLQS AGGELALDPL
DDEDAATVER LLRLHAEETG SQVATALLDD AAGWRHRFTR LLPLEYARIR RALDEAAQRG
LDPMAPGAWN EILELAHG
//