(data stored in SCRATCH3701 zone)

EMBL: CP001994.PE158

CP001994.PE158       Location/Qualifiers
FT   CDS             complement(189980..191881)
FT                   /codon_start=1
FT                   /transl_table=11
FT                   /locus_tag="Mmah_0161"
FT                   /product="phosphoadenosine phosphosulfate reductase"
FT                   /note="COGs: COG0175 3'-phosphoadenosine 5'-phosphosulfate
FT                   sulfotransferase (PAPS reductase)/FAD synthetase;
FT                   InterProIPR001450:IPR002478:IPR002500:IPR017900:IPR 004521;
FT                   KEGG: gem:GM21_0790 phosphoadenosine phosphosulfate
FT                   reductase; PFAM: phosphoadenosine phosphosulfate reductase;
FT                   PUA domain containing protein; 4Fe-4S ferredoxin
FT                   iron-sulfur binding domain protein; SMART: PUA domain
FT                   containing protein; SPTR: Q12UR6 Phosphoadenosine
FT                   phosphosulfate reductase; PFAM: PUA domain;
FT                   Phosphoadenosine phosphosulfate reductase family; TIGRFAM:
FT                   uncharacterized domain 2"
FT                   /db_xref="EnsemblGenomes-Gn:Mmah_0161"
FT                   /db_xref="EnsemblGenomes-Tr:ADE35696"
FT                   /db_xref="GOA:D5E945"
FT                   /db_xref="InterPro:IPR002478"
FT                   /db_xref="InterPro:IPR002500"
FT                   /db_xref="InterPro:IPR004521"
FT                   /db_xref="InterPro:IPR014729"
FT                   /db_xref="InterPro:IPR015947"
FT                   /db_xref="InterPro:IPR017896"
FT                   /db_xref="InterPro:IPR017900"
FT                   /db_xref="InterPro:IPR036974"
FT                   /db_xref="UniProtKB/TrEMBL:D5E945"
FT                   /protein_id="ADE35696.1"
FT                   /translation="MSQPVFHGDLLLQWCHSCNVAVLGKKCACGAECVKVNVTPPGDIR
FT                   PAFLHDIEHINRISKQQFNNPLLDTDRIVLLNKAPYEDRMDEVIVDGEVIASIRYEIGK
FT                   LEWVLLPRLEAARRIMAGKENLTGYVTIEDDVKIFLHKGANLLAPGVLDADSGIQKNDE
FT                   VIIITTAGEVVATGRARMDGQEMMEAQKGTAVKPRWKEDTTSKVNDRKPSCWDDVIRAN
FT                   RFIMDEAIGQAHDFIQKTIKKEELPISVSYSGGKDSLAVVQLVDECVGDYDIMFADTGL
FT                   EFPETLENIDHVGELYSKDVRSISVGEAFWDSIDAFGPPAVEMRWCCKICKLGPLSQLI
FT                   KENYDKGCLTFVGQRKYESTTRARSNRVWKNPWVGNQTAASPIQDWTALHIWLYIFMNE
FT                   LPYNPLYEKGFDRMGCWLCPSSSLGDLKRLKETHPHYEEKLMKHLYAYADKTGIDKEWA
FT                   DYGFWRWKSLPANIKKIAEELGINTAPTRYDPNKLTFTSSVGHRPCTTGEMTAEGSFST
FT                   VLDMEKIRKSGMLLAIGEVKYTDEMAMITRKKDTAQVFATGSVRVRASSKSDAGKLLRD
FT                   TESSIRRALGCTGCGVCIGKCPHNAIRIENKIAYIGDKCTHCGKCIEVCPVVKFIRD"
     MSQPVFHGDL LLQWCHSCNV AVLGKKCACG AECVKVNVTP PGDIRPAFLH DIEHINRISK        60
     QQFNNPLLDT DRIVLLNKAP YEDRMDEVIV DGEVIASIRY EIGKLEWVLL PRLEAARRIM       120
     AGKENLTGYV TIEDDVKIFL HKGANLLAPG VLDADSGIQK NDEVIIITTA GEVVATGRAR       180
     MDGQEMMEAQ KGTAVKPRWK EDTTSKVNDR KPSCWDDVIR ANRFIMDEAI GQAHDFIQKT       240
     IKKEELPISV SYSGGKDSLA VVQLVDECVG DYDIMFADTG LEFPETLENI DHVGELYSKD       300
     VRSISVGEAF WDSIDAFGPP AVEMRWCCKI CKLGPLSQLI KENYDKGCLT FVGQRKYEST       360
     TRARSNRVWK NPWVGNQTAA SPIQDWTALH IWLYIFMNEL PYNPLYEKGF DRMGCWLCPS       420
     SSLGDLKRLK ETHPHYEEKL MKHLYAYADK TGIDKEWADY GFWRWKSLPA NIKKIAEELG       480
     INTAPTRYDP NKLTFTSSVG HRPCTTGEMT AEGSFSTVLD MEKIRKSGML LAIGEVKYTD       540
     EMAMITRKKD TAQVFATGSV RVRASSKSDA GKLLRDTESS IRRALGCTGC GVCIGKCPHN       600
     AIRIENKIAY IGDKCTHCGK CIEVCPVVKF IRD                                    633
//

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