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Database: UniProt
Entry: A0A1I0ZP65_9CELL
LinkDB: A0A1I0ZP65_9CELL
Original site: A0A1I0ZP65_9CELL 
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
//
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