(data stored in SCRATCH9089 zone)

EMBL: CP002209.PE414

CP002209.PE414       Location/Qualifiers
FT   CDS             complement(452050..453642)
FT                   /codon_start=1
FT                   /transl_table=11
FT                   /locus_tag="Fbal_0414"
FT                   /product="IMP cyclohydrolase
FT                   ;phosphoribosylaminoimidazolecarboxamide formyltransferase"
FT                   /EC_number="3.5.4.10"
FT                   /EC_number="2.1.2.3"
FT                   /note="COGs: COG0138 AICAR transformylase/IMP
FT                   cyclohydrolase PurH (only IMP cyclohydrolase domain in
FT                   Aful); InterPro IPR011607: IPR013982: IPR002695; KEGG:
FT                   vfm:VFMJ11_2512 bifunctional
FT                   phosphoribosylaminoimidazolecarboxamide
FT                   formyltransferase/IMP cyclohydrolase; PFAM:
FT                   AICARFT/IMPCHase bienzyme formylation region; MGS domain
FT                   protein; PRIAM: IMP cyclohydrolase; SMART: AICARFT/IMPCHase
FT                   bienzyme formylation region; SPTR: B5FC70 Bifunctional
FT                   purine biosynthesis protein purH; TIGRFAM:
FT                   phosphoribosylaminoimidazolecarboxamide
FT                   formyltransferase/IMP cyclohydrolase; PFAM:
FT                   AICARFT/IMPCHase bienzyme; MGS-like domain; TIGRFAM:
FT                   phosphoribosylaminoimidazolecarboxamide
FT                   formyltransferase/IMP cyclohydrolase"
FT                   /db_xref="EnsemblGenomes-Gn:Fbal_0414"
FT                   /db_xref="EnsemblGenomes-Tr:ADN74628"
FT                   /db_xref="GOA:E1SNC9"
FT                   /db_xref="InterPro:IPR002695"
FT                   /db_xref="InterPro:IPR011607"
FT                   /db_xref="InterPro:IPR016193"
FT                   /db_xref="InterPro:IPR024051"
FT                   /db_xref="InterPro:IPR036914"
FT                   /db_xref="UniProtKB/TrEMBL:E1SNC9"
FT                   /protein_id="ADN74628.1"
FT                   /translation="MNAPRPIRRALLSVSDKTGIVEFARALSERGVELLSTGGTARLLA
FT                   DSGLNVTEVSDYTCFPEMMDGRVKTLHPKVHGGILGRREQDDAVMDSHGIKPIDMVVVN
FT                   LYPFAQTVAKAGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVNAHDYDRVITEMDAG
FT                   EGSLTFQTRFDLAIAAFEHTAAYDGMIANYFGTMVPSYGDNKEGDEESVFPRTFNQQFI
FT                   KKQDMRYGENSHQRAAFYVEKNVQEASVATAVQLQGKALSYNNIADTDAALECVKEFDV
FT                   PACVIVKHANPCGVALGDNILDAYDRAFKTDPTSAFGGIIAFNRELDGDTAKAIVDRQF
FT                   VEVIIAPSISADAKAIVADKKNVRLLACGQWESKTTEFDTKRVNGGLLVQDRDQGMVGL
FT                   DDIKVVSKRQPTAEQLQDLMFCWKVAKYVKSNAIVYAKDGMTVGVGAGQMSRVYSAKIA
FT                   GIKAADEGLTVPGSVMASDAFFPFRDGIDAAAEAGISCVIQPGGSMRDQEVIDAADEHG
FT                   MVMIFTNMRHFKH"
     MNAPRPIRRA LLSVSDKTGI VEFARALSER GVELLSTGGT ARLLADSGLN VTEVSDYTCF        60
     PEMMDGRVKT LHPKVHGGIL GRREQDDAVM DSHGIKPIDM VVVNLYPFAQ TVAKAGCTLE       120
     DAVENIDIGG PTMVRSAAKN HKDVAIVVNA HDYDRVITEM DAGEGSLTFQ TRFDLAIAAF       180
     EHTAAYDGMI ANYFGTMVPS YGDNKEGDEE SVFPRTFNQQ FIKKQDMRYG ENSHQRAAFY       240
     VEKNVQEASV ATAVQLQGKA LSYNNIADTD AALECVKEFD VPACVIVKHA NPCGVALGDN       300
     ILDAYDRAFK TDPTSAFGGI IAFNRELDGD TAKAIVDRQF VEVIIAPSIS ADAKAIVADK       360
     KNVRLLACGQ WESKTTEFDT KRVNGGLLVQ DRDQGMVGLD DIKVVSKRQP TAEQLQDLMF       420
     CWKVAKYVKS NAIVYAKDGM TVGVGAGQMS RVYSAKIAGI KAADEGLTVP GSVMASDAFF       480
     PFRDGIDAAA EAGISCVIQP GGSMRDQEVI DAADEHGMVM IFTNMRHFKH                  530
//

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