(data stored in ACNUC7421 zone)

EMBL: CP002116.PE210

CP002116.PE210       Location/Qualifiers
FT   CDS             216028..217680
FT                   /codon_start=1
FT                   /transl_table=11
FT                   /locus_tag="Spirs_0213"
FT                   /product="phosphoglycerate mutase,
FT                   2,3-bisphosphoglycerate-independent"
FT                   /note="COGs: COG0696 Phosphoglyceromutase; InterPro
FT                   IPR005995:IPR011258:IPR006124; KEGG: mca:MCA0753
FT                   phosphoglyceromutase; PFAM: BPG-independent PGAM domain
FT                   protein; metalloenzyme domain protein; PRIAM:
FT                   Phosphoglycerate mutase; SPTR: Phosphoglycerate mutase,
FT                   2,3-bisphosphoglycerate-independent; TIGRFAM:
FT                   phosphoglycerate mutase,
FT                   2,3-bisphosphoglycerate-independent; PFAM: Metalloenzyme
FT                   superfamily; BPG-independent PGAM N-terminus (iPGM_N);
FT                   TIGRFAM: 2,3-bisphosphoglycerate-independent
FT                   phosphoglycerate mutase"
FT                   /db_xref="EnsemblGenomes-Gn:Spirs_0213"
FT                   /db_xref="EnsemblGenomes-Tr:ADK79370"
FT                   /db_xref="GOA:E1RA79"
FT                   /db_xref="InterPro:IPR005995"
FT                   /db_xref="InterPro:IPR006124"
FT                   /db_xref="InterPro:IPR011258"
FT                   /db_xref="InterPro:IPR017850"
FT                   /db_xref="InterPro:IPR036646"
FT                   /db_xref="UniProtKB/TrEMBL:E1RA79"
FT                   /protein_id="ADK79370.1"
FT                   /translation="MVEALKANPAFSGRKGPVVLVIMDGVGFGKYTEGDAVAAAHTEVL
FT                   DELMASYPMTKLKAHGIAVGLPSDDDMGNSEVGHNAIGAGRVFAQGAKRVNGAIESGEM
FT                   FTGETWKKLTENVKKSGGSLHFLGLLSDGNVHSHINHLKAMVARAKEDGVKRVRVHALL
FT                   DGRDVGETSALDYFDPFADYLASLSDGGFDAKIASGGGRMKITMDRYNADWEMVHRGWQ
FT                   IHVLGEGRQFANAHEAIETLRKETGAIDQDLPPFVIAEGGKAVGTVEDGDSFILFNFRG
FT                   DRALEITKAFEAGDDFSEFDRVRVPNVEYAGMMEYDGDLHVPKQYLVSPPSIDKTMAEY
FT                   LAASGVKMFSISETQKFGHVTYFFNGNRSGKFSEELEEYVEIPSDRVPFEERPWMKAAE
FT                   ITDRVIEEIEKGSYRFIKLNYPNGDMVGHTGIYEAVLCSMEALDLSLGRLKKAVEKAGG
FT                   VMVISADHGNSDDMFEHDKKSGAVKTKANGKPQAKTSHSLNPVPCIVYDPGYKGEYAKE
FT                   LRSGLGISSLAATCIELLGFQAPEDYDTSVFTW"
     MVEALKANPA FSGRKGPVVL VIMDGVGFGK YTEGDAVAAA HTEVLDELMA SYPMTKLKAH        60
     GIAVGLPSDD DMGNSEVGHN AIGAGRVFAQ GAKRVNGAIE SGEMFTGETW KKLTENVKKS       120
     GGSLHFLGLL SDGNVHSHIN HLKAMVARAK EDGVKRVRVH ALLDGRDVGE TSALDYFDPF       180
     ADYLASLSDG GFDAKIASGG GRMKITMDRY NADWEMVHRG WQIHVLGEGR QFANAHEAIE       240
     TLRKETGAID QDLPPFVIAE GGKAVGTVED GDSFILFNFR GDRALEITKA FEAGDDFSEF       300
     DRVRVPNVEY AGMMEYDGDL HVPKQYLVSP PSIDKTMAEY LAASGVKMFS ISETQKFGHV       360
     TYFFNGNRSG KFSEELEEYV EIPSDRVPFE ERPWMKAAEI TDRVIEEIEK GSYRFIKLNY       420
     PNGDMVGHTG IYEAVLCSME ALDLSLGRLK KAVEKAGGVM VISADHGNSD DMFEHDKKSG       480
     AVKTKANGKP QAKTSHSLNP VPCIVYDPGY KGEYAKELRS GLGISSLAAT CIELLGFQAP       540
     EDYDTSVFTW                                                              550
//

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