(data stored in ACNUC7421 zone)

EMBL: CP002355.PE268

CP002355.PE268       Location/Qualifiers
FT   CDS             256186..258222
FT                   /codon_start=1
FT                   /transl_table=11
FT                   /locus_tag="Sulku_0269"
FT                   /product="FAD-dependent pyridine nucleotide-disulfide
FT                   oxidoreductase"
FT                   /note="COGs: COG0493 NADPH-dependent glutamate synthase
FT                   beta chain and related oxidoreductase; InterPro IPR000759:
FT                   IPR019575: IPR013027; KEGG: tdn:Suden_1824 glutamate
FT                   synthase (NADPH); PFAM: FAD-dependent pyridine
FT                   nucleotide-disulphide oxidoreductase; NADH ubiquinone
FT                   oxidoreductase, F subunit, iron sulphur binding; SPTR:
FT                   Formate dehydrogenase, beta subunit; PFAM: Pyridine
FT                   nucleotide-disulphide oxidoreductase; NADH-ubiquinone
FT                   oxidoreductase-F iron-sulfur binding region"
FT                   /db_xref="EnsemblGenomes-Gn:Sulku_0269"
FT                   /db_xref="EnsemblGenomes-Tr:ADR32936"
FT                   /db_xref="GOA:E4TYF9"
FT                   /db_xref="InterPro:IPR009051"
FT                   /db_xref="InterPro:IPR019575"
FT                   /db_xref="InterPro:IPR023753"
FT                   /db_xref="InterPro:IPR028261"
FT                   /db_xref="InterPro:IPR036188"
FT                   /db_xref="InterPro:IPR037207"
FT                   /db_xref="UniProtKB/TrEMBL:E4TYF9"
FT                   /protein_id="ADR32936.1"
FT                   /translation="MSKVYFSTWRGEQINNIGKNDDAWENSAYNLPLEYNEHAHSKAFI
FT                   GWDGVALFNPDVDVVRLATEYAAQYQVYSEACGRCAPGRWGGRILYDLLDKIARGEGSV
FT                   SDMEHLKEVSRTMQETSKCEIGKTVPNPLLDLMTHFESDFMDCINNQKPSKHYHLEDTS
FT                   YIAKITAPCMDACPAHVDIPAYIEGVRDLRFDDSLMATRQTMPLAHTCGRVCPHPCETE
FT                   CRRTNLDEPISIMELKRLGADYETDHGFGFFHPSEKKPSIGKKVAVIGAGPAGLTGAYY
FT                   LALDGIDVDVYEELPVLGGEVAVGVPEYRMPIDKYNQDIEAVRSLGVNFITNTKVTADM
FT                   MRQFENDYDATLVATGTRISKKVYCDNERPEIQGYWGAIDFLDKVNLQVKYDIMVPEAD
FT                   QKRHMLPTDFVDLTGKTLVCVGGGFTSMDVVRCAIRANAAKVVMLYRRDEATIIKNTTY
FT                   EEYHEAVEEGVEFIFHSAVAKMNDENDVLKSLVIDRFELVPDPNGGRPTLEKVEGASFE
FT                   MECDYLIPAVSQSADLKLLPEEWEIERTSWATIKTNGKDYMTSRKGIFAAGDCEYGPMT
FT                   IVNAVGQAKRAASVMSRYVTSGEITLTNDEIMEDHLRKLKVYNKKEKIQGWLPGLARQH
FT                   SEVLTVDERKDNNREVKYGFTQEEALAEAERCMRCYYIAMVAH"
     MSKVYFSTWR GEQINNIGKN DDAWENSAYN LPLEYNEHAH SKAFIGWDGV ALFNPDVDVV        60
     RLATEYAAQY QVYSEACGRC APGRWGGRIL YDLLDKIARG EGSVSDMEHL KEVSRTMQET       120
     SKCEIGKTVP NPLLDLMTHF ESDFMDCINN QKPSKHYHLE DTSYIAKITA PCMDACPAHV       180
     DIPAYIEGVR DLRFDDSLMA TRQTMPLAHT CGRVCPHPCE TECRRTNLDE PISIMELKRL       240
     GADYETDHGF GFFHPSEKKP SIGKKVAVIG AGPAGLTGAY YLALDGIDVD VYEELPVLGG       300
     EVAVGVPEYR MPIDKYNQDI EAVRSLGVNF ITNTKVTADM MRQFENDYDA TLVATGTRIS       360
     KKVYCDNERP EIQGYWGAID FLDKVNLQVK YDIMVPEADQ KRHMLPTDFV DLTGKTLVCV       420
     GGGFTSMDVV RCAIRANAAK VVMLYRRDEA TIIKNTTYEE YHEAVEEGVE FIFHSAVAKM       480
     NDENDVLKSL VIDRFELVPD PNGGRPTLEK VEGASFEMEC DYLIPAVSQS ADLKLLPEEW       540
     EIERTSWATI KTNGKDYMTS RKGIFAAGDC EYGPMTIVNA VGQAKRAASV MSRYVTSGEI       600
     TLTNDEIMED HLRKLKVYNK KEKIQGWLPG LARQHSEVLT VDERKDNNRE VKYGFTQEEA       660
     LAEAERCMRC YYIAMVAH                                                     678
//

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