(data stored in SCRATCH zone)

EMBL: CP002105.PE319

CP002105.PE319       Location/Qualifiers
FT   CDS             348652..349650
FT                   /codon_start=1
FT                   /transl_table=11
FT                   /locus_tag="Acear_0322"
FT                   /product="glyceraldehyde-3-phosphate dehydrogenase"
FT                   /EC_number="1.2.1.12"
FT                   /note="COGs: COG0057 Glyceraldehyde-3-phosphate
FT                   dehydrogenase/erythrose-4-phosphate dehydrogenase;
FT                   InterProIPR020830:IPR020832:IPR016040:IPR006424:IPR
FT                   020831:IPR020828:IPR020829; KEGG: sru:SRU_1200
FT                   glyceraldehyde-3-phosphate dehydrogenase, type I; PFAM:
FT                   Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding
FT                   domain; Glyceraldehyde 3-phosphate dehydrogenase, catalytic
FT                   domain; PRIAM: Glyceraldehyde-3-phosphate dehydrogenase
FT                   (phosphorylating); SPTR: Q2S3A6 Glyceraldehyde-3-phosphate
FT                   dehydrogenase, type I; TIGRFAM: glyceraldehyde-3-phosphate
FT                   dehydrogenase, type I; PFAM: Glyceraldehyde 3-phosphate
FT                   dehydrogenase, C-terminal domain; Glyceraldehyde
FT                   3-phosphate dehydrogenase, NAD binding domain; TIGRFAM:
FT                   glyceraldehyde-3-phosphate dehydrogenase, type I"
FT                   /db_xref="EnsemblGenomes-Gn:Acear_0322"
FT                   /db_xref="EnsemblGenomes-Tr:ADL11871"
FT                   /db_xref="GOA:D9QU78"
FT                   /db_xref="InterPro:IPR006424"
FT                   /db_xref="InterPro:IPR020828"
FT                   /db_xref="InterPro:IPR020829"
FT                   /db_xref="InterPro:IPR020830"
FT                   /db_xref="InterPro:IPR020831"
FT                   /db_xref="InterPro:IPR036291"
FT                   /db_xref="UniProtKB/TrEMBL:D9QU78"
FT                   /protein_id="ADL11871.1"
FT                   /translation="MTKKIAINGFGRIGRNIFRIIQQREDVDLEIVAINDLTDADNLAY
FT                   LLKYDSVHGRYDGEVEVGENGIKVDGKDYEVTSESDPANLDWSGKDIDIVIEATGVFRR
FT                   REQLEKHLKAGADKVVLTVPAKDKIDSTIVLGVNDDDLDESDQIVSNASCTTNCLAPMA
FT                   KVLNDEFGIEKGLITTVHGYTASQSILDAPAKKTRRGRTAAENIIPTTTGAAIATTKVL
FT                   PELEGKINGMAMRVPVPDGSVVDGVFDLETDVTVKEVNEAFKKAAEGEMEGILGYTEDE
FT                   LVSRDIIGSPYSSLIDAQSTMMIANNQIKVLSWYDNEWGYSNRVIELADRL"
     MTKKIAINGF GRIGRNIFRI IQQREDVDLE IVAINDLTDA DNLAYLLKYD SVHGRYDGEV        60
     EVGENGIKVD GKDYEVTSES DPANLDWSGK DIDIVIEATG VFRRREQLEK HLKAGADKVV       120
     LTVPAKDKID STIVLGVNDD DLDESDQIVS NASCTTNCLA PMAKVLNDEF GIEKGLITTV       180
     HGYTASQSIL DAPAKKTRRG RTAAENIIPT TTGAAIATTK VLPELEGKIN GMAMRVPVPD       240
     GSVVDGVFDL ETDVTVKEVN EAFKKAAEGE MEGILGYTED ELVSRDIIGS PYSSLIDAQS       300
     TMMIANNQIK VLSWYDNEWG YSNRVIELAD RL                                     332
//

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