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Database: UniProt
Entry: F2NLB0_MARHT
LinkDB: F2NLB0_MARHT
Original site: F2NLB0_MARHT 
ID   F2NLB0_MARHT            Unreviewed;       627 AA.
AC   F2NLB0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Glutamine amidotransferase of anthranilate synthase {ECO:0000313|EMBL:AEB11729.1};
DE            EC=4.1.3.27 {ECO:0000313|EMBL:AEB11729.1};
GN   OrderedLocusNames=Marky_0986 {ECO:0000313|EMBL:AEB11729.1};
OS   Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Marinithermus.
OX   NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB11729.1, ECO:0000313|Proteomes:UP000007030};
RN   [1] {ECO:0000313|EMBL:AEB11729.1, ECO:0000313|Proteomes:UP000007030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX   PubMed=22675595; DOI=10.4056/sigs.2435521;
RA   Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA   Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J.,
RA   Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT   hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT   chimney.";
RL   Stand. Genomic Sci. 6:21-30(2012).
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DR   EMBL; CP002630; AEB11729.1; -; Genomic_DNA.
DR   RefSeq; WP_013703777.1; NC_015387.1.
DR   AlphaFoldDB; F2NLB0; -.
DR   STRING; 869210.Marky_0986; -.
DR   MEROPS; C26.955; -.
DR   KEGG; mhd:Marky_0986; -.
DR   eggNOG; COG0147; Bacteria.
DR   eggNOG; COG0512; Bacteria.
DR   HOGENOM; CLU_006493_5_0_0; -.
DR   OrthoDB; 9803598at2; -.
DR   Proteomes; UP000007030; Chromosome.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF9; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF56322; ADC synthase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW   ECO:0000313|EMBL:AEB11729.1}; Lyase {ECO:0000313|EMBL:AEB11729.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007030}.
FT   DOMAIN          150..401
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   DOMAIN          442..618
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        514
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        601
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        603
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   627 AA;  68561 MW;  9C524944D692B4A6 CRC64;
     MEALGLYRRA RALGLRPALL ESLGPRTAFG RRTLLGLRPT RRLEVWGGVL YEDGRLVGTA
     LDLLERLEEG LGEGHFPAWI GFFAYEFARH LGLPARAPMP GLPEAAFCYY PEGYVWEDGR
     LVEAPSVLLE VDPGMPVGLP EVRLVSDYPR EAFIAGVQAV QERIRAGWVY QVNLSHRFRF
     PAVGLDPLDY YAALRRTNPS PFMGLVEGAG WAVVSGSPER LFALREGVLS ARPIAGTRRR
     GRTPEEDQAL EAELRANVKE RAEHVMLVDL LRNDLSRVAE PGTVEVSEAF TVERYSHVMH
     LVSEVRGVSR AGVGAALRAI FPGGTITGAP KESVMQAIAE LEPVPRGAYT GSLGYVSGRG
     ADFNILIRSL TLAGGWAYLS AGAGIVIESD PVREYEETRH KAEALLYVLG QGRPGVRPEP
     PRVIEAWRPP RPRRRYAARV VFLENHDSFS YNLVNYLRML GAEVRVVDHG EPPALGGATH
     LVVGPGPGDP FTAGRTLEWV RAALEDGVPF LGVCLGHQAL GVALGAVLER APRPVHGEAH
     PVRHVGRGVF AGLPDPAPFT RYHSLHLRDL PPVLERLAWT EDGVVMGVGH RSRPAWGVQF
     HPESMLSPYG LELLANFLEV RGAAGDR
//
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