(data stored in SCRATCH zone)

SWISSPROT: C5DCP3_LACTC

ID   C5DCP3_LACTC            Unreviewed;      2159 AA.
AC   C5DCP3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   SubName: Full=KLTH0B04708p {ECO:0000313|EMBL:CAR21554.1};
GN   OrderedLocusNames=KLTH0B04708g {ECO:0000313|EMBL:CAR21554.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21554.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21554.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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DR   EMBL; CU928166; CAR21554.1; -; Genomic_DNA.
DR   RefSeq; XP_002551992.1; XM_002551946.1.
DR   STRING; 381046.XP_002551992.1; -.
DR   PRIDE; C5DCP3; -.
DR   EnsemblFungi; CAR21554; CAR21554; KLTH0B04708g.
DR   GeneID; 8290829; -.
DR   KEGG; lth:KLTH0B04708g; -.
DR   HOGENOM; HOG000031559; -.
DR   InParanoid; C5DCP3; -.
DR   KO; K00264; -.
DR   OMA; RFKTGAM; -.
DR   OrthoDB; 126283at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR   CDD; cd00982; gltB_C; 1.
DR   CDD; cd02808; GltS_FMN; 1.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 2.160.20.60; -; 1.
DR   Gene3D; 3.20.20.70; -; 2.
DR   Gene3D; 3.50.50.60; -; 2.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
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; IPR012220; Glu_synth_euk.
DR   InterPro; IPR002932; Glu_synthdom.
DR   InterPro; IPR006005; Glut_synth_ssu1.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   Pfam; PF14691; Fer4_20; 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   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF000187; GOGAT; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   SUPFAM; SSF69336; SSF69336; 1.
DR   TIGRFAMs; TIGR01317; GOGAT_sm_gam; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   4: Predicted;
DR   PRODOM; C5DCP3.
DR   SWISS-2DPAGE; C5DCP3.
KW   3Fe-4S {ECO:0000256|PIRSR:PIRSR000187-2};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Iron {ECO:0000256|PIRSR:PIRSR000187-2};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR000187-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000187-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT   DOMAIN       65    472       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   COILED     1636   1656       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     65     65       For GATase activity. {ECO:0000256|PIRSR:
FT                                PIRSR000187-1}.
FT   METAL      1202   1202       Iron-sulfur (3Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000187-2}.
FT   METAL      1208   1208       Iron-sulfur (3Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000187-2}.
FT   METAL      1213   1213       Iron-sulfur (3Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000187-2}.
SQ   SEQUENCE   2159 AA;  238558 MW;  1A6F2307A0B609A4 CRC64;
     MLRSDEFDPL QEAYDGGMPL DTRRMHSDDS DINGFGASSK DSQFWADAIP GKQGLYDPEY
     ERDACGVGFV ANIKGAQSHK IVSDARYLLC NMTHRGAVSS GGNGDGAGIL VGIPHEFMKR
     EFRLDSGIEI PAAGQYATGN FFFKKDAPET LEASKRTFES LAESLGLLVL GWRSVPRDSS
     ILGAVALSRE PAIFQPLVVL QEAHHEQQPI SAQDFREKFD VKFQTQLYIL RKQASSAIGL
     QNWFYACSLN PRTIVYKGQL TPTQVYQYYH DLTNAHFESH MALVHSRFST NTFPSWDRAQ
     PLRWIAHNGE INTLRGNKNW MRAREGVMAS ETFGEQLDKL YPIIEEGGSD SAALDNVLEL
     LVINGALSLP EAIMMMVPEA YHKDMDSNLK AWFDWSACLM EPWDGPALLT FTDGRYCGAM
     LDRNGLRPCR YYITSDDRVI CASEVGVIPV DNSLVVQKGK LKPGDMLLVD TDLGEMVDTK
     KLKSTFSKKR DYKSWLSKLI KLEDLLVKTQ KYIPDSFLSD RHASLKAQQD PRLLAMGYTF
     EQVSMVLIPM ALGSKEALGS MGNDAPLACL NENPVLIYDY FRQLFAQVTN PPIDPIREAN
     VMSLECYVGP QGNLLEVHPS QCDRLLLHSP ILQWREFEAI KNIEKAHPAW SVADIDITFE
     KSQGLLGYTS TIERITHQAS EAIEQGKRII MISDRRMGPD RVPLSSLIAV GAIHHHLIRN
     KQRSQVALIL ETGEAREVHH FCVLLGYGCD GIFPYLAMET LVRMNQEDLV RNVENDDIDI
     DDTTLLENYK HAIDGGILKV MSKMGISTLA SYKGAQIFEA LGVDNTVVDL CFAGTASRIQ
     GVTFEYIAQD AFSMHERGFP SRFTISKSVN LPESGEYHWR DGGAKHINDP TAIASLQDSV
     RNKNSNAWEM YVKKEMESIR DCTLRGLLEL DFENSESIPL EQVEPWTEIA RRFATGAMSY
     GSISMEAHST LAVAMNRLGA KSNCGEGGED AERSIVHSNG DTMRSAIKQV ASARFGVTSH
     YLSDADEIQI KIAQGAKPGE GGELPAHKVS PDIAKTRHST PYVGLISPPP HHDIYSIEDL
     KQLIYDLKCS NPRAGISVKL VSEVGVGIVA SGVAKAKADH ILVSGHDGGT GASRWTGIKY
     AGLPWELGLA ETHQTLVLND LRRNVVVQTD GQLRTGFDIA VAVLLGAESF TLATVPLIAM
     GCIMLRKCHL NACAVGIATQ DPLLREKFKG QPEHVINFFY YLIQDLRKIM AKLGFRTIDE
     MVGHSEKLRK RENVNTKAIN IDLSPILTPA HVIRPGVATK FTKKQDHRLH TRLDNKLIDE
     AEITLDRGLP VNIDATIINT DRALGSTLSY RISKKFGEEG LPQDTVVVNI EGSAGQSFGA
     FLASGITFIL DGDANDYVGK GLSGGRLIIR PPPDSRFKSD ENVILGNTCF YGATSGTAFI
     SGVAGERFCV RNSGATIVVE KIKGNNAFEY MTGGRAVVLS QMESLNAFSG ATGGIAYCLT
     SDYDDFVGKI NTESVELQGL IDPVEIAFVK NLIQEHYNYT KSELAARILG NFNHYLKNFV
     KVIPTDYKKV LEKDAEEKAK LKQKNTANFL KKFNSGTDLK SDVTNGEVDA IREAKKKAVR
     NISHKATLAE PKVQDLEDAV NDIEQLEKNG EKIQKTRGFM LYKLRHEKYR HASARTKDWK
     ELSACVTKKD AKYQTARCMD CGVPFCTSDT GCPISNVIPK FNELVFKNQW KLALDKLLET
     NNFPEFTGRV CPAPCQGSCT LGIIDDPVGI KSIERLIIDN GFKEGWIQPC PPEVRTGRNI
     AIIGSGPAGL ACADQLNRAG HSVTVYERAD RCGGLLMYGI PNMKLDKKIV QRRVDLMAAE
     GVEFVTSVEI GKDITVEQLK AQNDAVVYAI GSTIPRDLRI PGRDLKNIDF AMSLLTANTK
     ALLSKDLETI RQQISGKKVI VIGGGDTGND CLGTSVRHGA ASVINFELLP QPPNERASDN
     PWPQWPRVMR VDYGHAEVKA HYGRDPREYC ILSKEFIGNE EGEVKAIRTV RVEWKRSESG
     VWQMVEVPGS EEIYEADVVL LSMGFVGPEL FEDPSVVKTK RGTINTVSDA SYSVDDGKVF
     AAGDCRRGQS LIVWAIQEGR KCATSVDSFL MGSTSLPGNG GIVKRDYRLL EELASTVEA
//

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