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Database: UniProt
Entry: A7TKZ5_VANPO
LinkDB: A7TKZ5_VANPO
Original site: A7TKZ5_VANPO 
ID   A7TKZ5_VANPO            Unreviewed;      2139 AA.
AC   A7TKZ5;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   05-JUN-2019, entry version 77.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDO17051.1};
GN   ORFNames=Kpol_530p21 {ECO:0000313|EMBL:EDO17051.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294)
OS   (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO17051.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M.,
RA   Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two
RT   yeast species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000187-2};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|PIRSR:PIRSR000187-2};
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DR   EMBL; DS480411; EDO17051.1; -; Genomic_DNA.
DR   RefSeq; XP_001644909.1; XM_001644859.1.
DR   STRING; 36033.XP_001644909.1; -.
DR   EnsemblFungi; EDO17051; EDO17051; Kpol_530p21.
DR   GeneID; 5545243; -.
DR   KEGG; vpo:Kpol_530p21; -.
DR   eggNOG; KOG0399; Eukaryota.
DR   eggNOG; COG0067; LUCA.
DR   eggNOG; COG0069; LUCA.
DR   eggNOG; COG0070; LUCA.
DR   eggNOG; COG0493; LUCA.
DR   InParanoid; A7TKZ5; -.
DR   KO; K00264; -.
DR   OMA; RFKTGAM; -.
DR   OrthoDB; 126283at2759; -.
DR   PhylomeDB; A7TKZ5; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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:EnsemblFungi.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019676; P:ammonia assimilation cycle; IEA:EnsemblFungi.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:EnsemblFungi.
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;
KW   3Fe-4S {ECO:0000256|PIRSR:PIRSR000187-2};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000267};
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:UP000000267}.
FT   DOMAIN       55    452       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   REGION        1     23       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A7TKZ5}.
FT   COILED     1550   1570       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     55     55       For GATase activity. {ECO:0000256|PIRSR:
FT                                PIRSR000187-1}.
FT   METAL      1184   1184       Iron-sulfur (3Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000187-2}.
FT   METAL      1190   1190       Iron-sulfur (3Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000187-2}.
FT   METAL      1195   1195       Iron-sulfur (3Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000187-2}.
SQ   SEQUENCE   2139 AA;  236861 MW;  18F800BCCDFC7FCB CRC64;
     MTVLSSEPFD PLQESYEGGA PMQLDSSVSH NNVSWSNVIP DKVGLYDPDY EKDACGVGFV
     SNIKGLQSHK IVADARFLLC NMTHRGAVSS DGNGDGAGIL VGIPHEFMKR EFKLDLGIDI
     PERGSYAVGN VFFKKDAPNT YLCASKKIFE DMASQLNLKV LGWRKVPCDS SILGQVALSR
     EPTILQPLVV TNDIDFSSSS LDFQTSLYLL RKRATSSIGI SNGFYVCSLS NTTIVYKGQL
     TPAQVYNYYP DLTNAYFKSH MALVHSRFST NTFPSWDRAQ PLRWLAHNGE INTLRGNKNW
     MRAREGVMFS ETFKEKIDQL YPIIEEGGSD SAALDNVLEL LTINGVLSLP EAIMLLVPEA
     YHKDMDSNLK AWFDWAACLM EPWDGPALLT FTDGRYIGAM LDRNGLRPCR YYVTNDDRVI
     CASEVGVIPI ENSLVVQKGK LKPGDLFLVD TQVGEIVDTK KLKLQFSKKK DFKSWLSKVI
     KLEDILEKLT DVIPTQFLSD NELTDSLKVN SDPRLLANGY TFEQVSMLLT PMALTGKEAL
     GSMGNDAPLA CLNEDPVLVY DYFRQLFAQV TNPPIDPIRE ANVMSLECYV GPQGNLLEMN
     SSQCNRLFLK SPILHWNEFS AIKNIEKVHP SWQIGNIDIT FDKSLGLLGY TDTIERITQE
     ATDYLDEGKK IIVISDRSLG PNRVAISSLI AVGAIHHHLV RNKQRSHVAL ILETAEAKEI
     HHFCVLLGYG CDGIFPYLAM ETLVRMNNEG LVRNVENDNK DIDNRTLLEN YKHAIDSGIL
     KVMSKMGIST LASYKGAQIF EALGLDNSVV DLCFAGTASR IKGVTFEYIA QDAFSLHERG
     WPSRSIISKS INLPESGEYH FRDGGYKHIN EPTAIASLQD SVRNKNEDAW AMYVRKEMEA
     IRDCTLRGLL ELDFENSSPI PLEQVEPWTE IARRFATGAM SYGSISMEAH STLAIAMNRL
     GAKSNCGEGG EDAERSIVSP NGDTMRSAIK QVASARFGVT SFYLSDADEI QIKVAQGAKP
     GEGGELPAHK VSKEIAKTRH STPYVGLISP PPHHDIYSIE DLKQLIYDLK CSNPRAGISV
     KLVSEVGVGI VASGVAKAKA DHILVSGHDG GTGAARWTSV KYAGLPWELG LAETHQTLVL
     NDLRRNVIVQ TDGQLRTGFD IAVAVLLGAE SFTLATIPLI AMGCVMLRRC HLNSCAVGIA
     TQDPYLRSKF KGQPEHVINF FYYLIQDLRK IMAKLGYRTI DEMVGHSEKL RKREDVSTKA
     INIDLSPILT AAHTIRPGVP TRFTKKQDMK LHTRLDNKLI DESEVTLDRG LPVNIDASII
     NTDRALGATL SYRVSKKFGE NGLPRDTIVV NISGSAGQSF GAFLASGVTF ILDGDANDYV
     GKGLSGGIIV IRPPATSNYR SDENVIVGNT CFYGATSGKA FISGSAGERF AVRNSGATIV
     IERIKGNNAF EYMTGGRAVV LSQMESLNAF SGATGGIAYC LTSDYDDFEG KINKETVCLE
     TLKDPVEIAF VKNLIQEHYN FTKSKLASKI LNNFNHYLKD FVKVIPTDYK KVLEKEAEEK
     VKEKQLKTAE FLKRFERSPN ENIVDATNGE IDEILSAKQK KYTVSHKSTL HEPKLLDLED
     SVPDAKQLEK NVEKVEKVRG FMKYKVRHEA YRKPSSRTKD WKEISDSITK KDAKYQTARC
     MDCGTPFCLS DTGCPISNII PKFNELVFKN QWKLALDKLS ETNNFPEFTG RVCPAPCQGA
     CTLGIIEDPV GIKSVERLII DNAFKEGWIK PCPPEVRTNR SIAIIGSGPA GLACADQLNK
     AGHNVTVYER ADRCGGLLMY GIPNMKLDKS IVQRRVDLLA AEGINFVVNT EIGKDITTDQ
     LKQQYDSVVY AIGSTIPRDL NIKGRELKNI DFAMTLLKSN TEALLNQDLE TIRKTIEGKK
     VVVIGGGDTG NDCLGTAVRH GASSVLNFEL LPQPPKERAK DNPWPQWPRV MRVDYGHAEV
     KEHYGRDPRE YCILSKEFIG NEEGEVTAIK TVRVEWKKSE SGVWQMIELP GSEEIIEADI
     VLLSMGFVGP ELFDDPNVAK TKRGTIATIN DSSYLIEDNV FATGDCRRGQ SLIVWAIQEG
     RKCAASIDQH LMGNTYLPSN GGIVKRDFNL LEELASKIN
//
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