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Desulfotomaculum reducens MI-1 (dred0)
Gene : ABO48913.1
DDBJ      :             dihydrolipoamide dehydrogenase
Swiss-Prot:             

Homologs  Archaea  65/68 : Bacteria  880/915 : Eukaryota  194/199 : Viruses  0/175   --->[See Alignment]
c.3.1d.87.1
:458 amino acids
:SECSTR
:PSIPRED
:BLT:PDB   1->33 2i0zA PDBj 1e-05 51.5 %
:BLT:PDB   19->449 1ebdA PDBj 3e-98 44.0 %
:RPS:PDB   3->457 1bhyA PDBj 3e-89 31.6 %
:RPS:SCOP  3->365 1gosA1  c.3.1.2 * 8e-39 13.6 %
:RPS:SCOP  338->453 1xdiA2  d.87.1.1 * 2e-36 32.8 %
:HMM:SCOP  1->332 1gpeA1 c.3.1.2 * 1.6e-65 32.3 %
:HMM:SCOP  335->457 1aogA3 d.87.1.1 * 6.1e-41 54.5 %
:RPS:PFM   4->306 PF07992 * Pyr_redox_2 2e-24 34.8 %
:RPS:PFM   339->447 PF02852 * Pyr_redox_dim 2e-32 57.8 %
:HMM:PFM   4->309 PF07992 * Pyr_redox_2 1.2e-49 41.3 196/202  
:HMM:PFM   339->448 PF02852 * Pyr_redox_dim 6.1e-43 52.7 110/110  
:BLT:SWISS 3->448 DLDH_CHLTR e-107 44.6 %
:PROS 37->47|PS00076|PYRIDINE_REDOX_1
:TM

SeqInfo AminoSeq See neighboring genes
Links GIB DAD Abbreviations Back to title page
GT:ID ABO48913.1 GT:GENE ABO48913.1 GT:PRODUCT dihydrolipoamide dehydrogenase GT:DATABASE GIB00494CH01 GT:ORG dred0 GB:ACCESSION GIB00494CH01 GB:LOCATION 386969..388345 GB:FROM 386969 GB:TO 388345 GB:DIRECTION + GB:PRODUCT dihydrolipoamide dehydrogenase GB:NOTE TIGRFAM: dihydrolipoamide dehydrogenase PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glucose-inhibited division protein A; pyridine nucleotide-disulphide oxidoreductase dimerisation region; HI0933 family protein KEGG: mta:Moth_1763 dihydrolipoamide dehydrogenase GB:PROTEIN_ID ABO48913.1 GB:DB_XREF GI:134050942 InterPro:IPR000103 InterPro:IPR000815 InterPro:IPR001100 InterPro:IPR001327 InterPro:IPR002218 InterPro:IPR004099 InterPro:IPR004792 InterPro:IPR006258 InterPro:IPR012999 InterPro:IPR013027 LENGTH 458 SQ:AASEQ MIYDAVVIGGGPGGYVAAIRIAQKGGKVAVIEKDQLGGTCLNRGCIPTKALIASVDKLKAVEEASEFGIEVGKPVIDFRKVQARKAEIVDKLVSGIKYLFDKNKIDHLNGTGKIKTANIVEVNNADKTYELQCKNIIVATGSSPSLIQSLGYNGTTIITSEEALKLTEVPKSLLIIGAGVIGCEFAHIFGSMGTQITMVEAAPSILSIQDKDISRRMQTVFKKKKFNIKTNVAITKMEQTGAGIQAELENGDIIKAEKALISIGRQLNTKNLGLEDIGVQLGEKGQILVNDRLETNIKGIYAVGDVISKYQLAHVASAQGIVAAENIMGKESTMDYNAVPSCIFTSPEISSVGITEQQAKDRKIPVKTGKFNFMANGKALSMGEGEGFVKIVAHKETDVVLGVHIIGPHASDLIAEATLAVRKGLTTKELAVTIHAHPTLAEVIMEAAENVHGLNIHG GT:EXON 1|1-458:0| BL:SWS:NREP 1 BL:SWS:REP 3->448|DLDH_CHLTR|e-107|44.6|444/465| PROS 37->47|PS00076|PYRIDINE_REDOX_1|PDOC00073| TM:NTM 3 TM:REGION 2->24| TM:REGION 137->159| TM:REGION 168->190| BL:PDB:NREP 2 BL:PDB:REP 1->33|2i0zA|1e-05|51.5|33/416| BL:PDB:REP 19->449|1ebdA|3e-98|44.0|430/455| RP:PDB:NREP 1 RP:PDB:REP 3->457|1bhyA|3e-89|31.6|455/482| RP:PFM:NREP 2 RP:PFM:REP 4->306|PF07992|2e-24|34.8|264/275|Pyr_redox_2| RP:PFM:REP 339->447|PF02852|2e-32|57.8|109/110|Pyr_redox_dim| HM:PFM:NREP 2 HM:PFM:REP 4->309|PF07992|1.2e-49|41.3|196/202|Pyr_redox_2| HM:PFM:REP 339->448|PF02852|6.1e-43|52.7|110/110|Pyr_redox_dim| GO:PFM:NREP 5 GO:PFM GO:0005737|"GO:cytoplasm"|PF02852|IPR004099| GO:PFM GO:0016491|"GO:oxidoreductase activity"|PF02852|IPR004099| GO:PFM GO:0045454|"GO:cell redox homeostasis"|PF02852|IPR004099| GO:PFM GO:0050660|"GO:FAD binding"|PF02852|IPR004099| GO:PFM GO:0055114|"GO:oxidation reduction"|PF02852|IPR004099| RP:SCP:NREP 2 RP:SCP:REP 3->365|1gosA1|8e-39|13.6|359/385|c.3.1.2| RP:SCP:REP 338->453|1xdiA2|2e-36|32.8|116/118|d.87.1.1| HM:SCP:REP 1->332|1gpeA1|1.6e-65|32.3|319/0|c.3.1.2|1/1|FAD/NAD(P)-binding domain| HM:SCP:REP 335->457|1aogA3|6.1e-41|54.5|123/130|d.87.1.1|1/1|FAD/NAD-linked reductases, dimerisation (C-terminal) domain| OP:NHOMO 4495 OP:NHOMOORG 1139 OP:PATTERN 22111284666777762431311541122351232331222212212111332212332223442--- 4455743455633394566-8611876666635555379835455535455256A4443355B4645553212222221-123131114442-422122222273332321111111111111132313322222333312111434444444123322222322245474222222222222422443211535555554535565454644535552424377544444553555554544555444A786434165123228A33554557635556445444554444433444444444444444444555444555542413555555555327332233422-23-11-64152236235545134216533433333466343343333344454454445-4454654867435664668666773A66555444445653333333353324544223222222211222222222222222221535724545868887964444773555553466648582345435366535452366311133333333357364226612532345333-324256451333344131111------------------213665567854535722222252422332223341-1764611111153345335556566655-5555565545565454555555443334444465455375545444444453145555555555511331111144542475522222222222222265556455543367785555455564443544445344344565555564655433443423322222233443333111-11-131312123-2-42111222132132---2212341434541 4411225-D55-2222222122223222222222212222222221333335582223222222222222222234323322222222-53222222222222425-3B676745665655565FD3G2Q*9-B8K3344A56764655454595A8676BF37522533766954554*44455697B284AA88679 ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- STR:NPRED 458 STR:RPRED 100.0 SQ:SECSTR ccEEEEEEcccHHHHHHHHHHHHTTccEEEEEccccccHHHHHHcHHHHHHHHHHHHHHHHHHGGGGTcccccccccHHHHHHHHHHHHHHHHHHHHHHHHHTTcEEEEEEEEEEETTEEEEEEEEEEEEEEEEEEEEEcccEEEcccccccccTTEEcHHHHTTccccccEEEEEcccHHHHHHHHHHHHHTcEEEEEcccccccTTccHHHHHHHHHHHGGGEEEEEcccEEEEEEEETTEEEEEEEccccEEEccEEEcccEEEcGGGTTGGGTTccccTTccccccTTcccccTTEEEcGGGTcccccHHHHHHHHHHHHHHHTTcccccccccccEEEcccccEEEEEccHHHHHHHTccEEEEEEEGGGcHHHHHTTccccEEEEEEETTTccEEEEEEEcTTHHHHHHHHHHHHHTTccHHHHHTccccccccTTHHHHHHHHHHTccTTc PSIPRED ccccEEEEcccHHHHHHHHHHHHcccEEEEEEccccccEEEEcccccHHHHHHHHHHHHHHHHcccccEEccccEEcHHHHHHHHHHHHHHHHHHHHHHHHHcccEEEEEEEEEEEccEEEEEccccEEEEEEEEEEEEccccccccccccccccEEEEHHHHHcHHHcccEEEEEcccHHHHHHHHHHHHcccEEEEEEccccccccccHHHHHHHHHHHHHcccEEEcccEEEEEEEcccEEEEEEccccEEEEcEEEEEccEEEcccccccHHcccEEcccccEEEccEEEcccccEEEEEEccccccccHHHHHHHHHHHHHHcccccccccccccEEEEEcccEEEEEccHHHHHHccccEEEEEEEcccccEEEcccccEEEEEEEEEccccEEEEEEEEEccHHHHHHHHHHHHHccccHHHHHccccccccHHHHHHHHHHHHccccccc //