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Eggerthella lenta DSM 2243 (elen0)
Gene : ACV54937.1
DDBJ      :             D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding
Swiss-Prot:             

Homologs  Archaea  49/68 : Bacteria  718/915 : Eukaryota  166/199 : Viruses  0/175   --->[See Alignment]
c.2.1c.23.12c.91.1d.58.18
:391 amino acids
:SECSTR
:PSIPRED
:BLT:PDB   20->390 2p9eD PDBj 2e-30 29.1 %
:RPS:PDB   20->303 3ba1A PDBj 4e-40 17.1 %
:RPS:PDB   322->389 2dtjA PDBj 1e-05 11.8 %
:RPS:SCOP  31->304 1aq2A1  c.91.1.1 * 7e-20 8.4 %
:RPS:SCOP  319->391 1ygyA3  d.58.18.1 * 3e-10 23.6 %
:HMM:SCOP  1->113 1dxyA2 c.23.12.1 * 4.1e-19 39.1 %
:HMM:SCOP  82->273 1psdA1 c.2.1.4 * 7.3e-39 29.9 %
:HMM:SCOP  306->391 1psdA3 d.58.18.1 * 3.2e-15 25.0 %
:RPS:PFM   23->297 PF00389 * 2-Hacid_dh 1e-15 28.5 %
:HMM:PFM   116->272 PF02826 * 2-Hacid_dh_C 2.4e-38 30.3 155/178  
:HMM:PFM   322->382 PF01842 * ACT 2.2e-06 19.7 61/66  
:BLT:SWISS 48->381 SERA_SCHPO 2e-30 30.5 %
:PROS 138->165|PS00065|D_2_HYDROXYACID_DH_1
:SEG

SeqInfo AminoSeq See neighboring genes
Links DAD Abbreviations Back to title page
GT:ID ACV54937.1 GT:GENE ACV54937.1 GT:PRODUCT D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding GT:DATABASE GIB01015CH01 GT:ORG elen0 GB:ACCESSION GIB01015CH01 GB:LOCATION complement(1170859..1172034) GB:FROM 1170859 GB:TO 1172034 GB:DIRECTION - GB:PRODUCT D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding GB:NOTE PFAM: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase catalytic region; amino acid-binding ACT domain protein; KEGG: bcb:BCB4264_A3260 putative D-3- phosphoglycerate dehydrogenase GB:PROTEIN_ID ACV54937.1 GB:DB_XREF GI:257474617 InterPro:IPR002912 InterPro:IPR006139 InterPro:IPR006140 LENGTH 391 SQ:AASEQ MRNIHCLNNISAYGTDLFTDDYELIDALDQAEGVLVRSAALHDTAFPDSLLAIARAGAGVNNIPLDRCAEEGIVVFNTPGANANAVKEIVVCGLMLGSRDIAGGIAWCRHNADDENIAKAAEKAKKAFAGREVKGKKLGVIGLGAIGAEVANIAIDLGMDVYGYDPYVSVGAAWRISSAVHHVTNLDDIFRTCGYMTIHVPAMDGTIGMIDERACSLMKDGAVFLNFSRDTLVDNAAMAAALDSGKVHAYITDFATPEVMKMERAIVLPHLGASTAEAEDNCAMMAVRELMDYLENGNIANSVNYPACDMGPVPDGLRRVAVLHANVPNAIARITNVFGDAGVNIENMMNKARGENAYTMLDLDAGTPGHPDDAIERLSAIEGVRRVRVVK GT:EXON 1|1-391:0| BL:SWS:NREP 1 BL:SWS:REP 48->381|SERA_SCHPO|2e-30|30.5|315/466| PROS 138->165|PS00065|D_2_HYDROXYACID_DH_1|PDOC00063| SEG 118->129|akaaekakkafa| SEG 132->151|evkgkklgviglgaigaeva| BL:PDB:NREP 1 BL:PDB:REP 20->390|2p9eD|2e-30|29.1|351/403| RP:PDB:NREP 2 RP:PDB:REP 20->303|3ba1A|4e-40|17.1|269/312| RP:PDB:REP 322->389|2dtjA|1e-05|11.8|68/164| RP:PFM:NREP 1 RP:PFM:REP 23->297|PF00389|1e-15|28.5|263/300|2-Hacid_dh| HM:PFM:NREP 2 HM:PFM:REP 116->272|PF02826|2.4e-38|30.3|155/178|2-Hacid_dh_C| HM:PFM:REP 322->382|PF01842|2.2e-06|19.7|61/66|ACT| GO:PFM:NREP 3 GO:PFM GO:0008152|"GO:metabolic process"|PF00389|IPR006139| GO:PFM GO:0016616|"GO:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor"|PF00389|IPR006139| GO:PFM GO:0051287|"GO:NAD or NADH binding"|PF00389|IPR006139| RP:SCP:NREP 2 RP:SCP:REP 31->304|1aq2A1|7e-20|8.4|250/310|c.91.1.1| RP:SCP:REP 319->391|1ygyA3|3e-10|23.6|72/78|d.58.18.1| HM:SCP:REP 1->113|1dxyA2|4.1e-19|39.1|110/0|c.23.12.1|1/1|Formate/glycerate dehydrogenase catalytic domain-like| HM:SCP:REP 82->273|1psdA1|7.3e-39|29.9|177/0|c.2.1.4|1/1|NAD(P)-binding Rossmann-fold domains| HM:SCP:REP 306->391|1psdA3|3.2e-15|25.0|84/0|d.58.18.1|1/1|ACT-like| OP:NHOMO 1439 OP:NHOMOORG 933 OP:PATTERN 11211111--------2------121111111111111111111111111111-1111112--1--11 112-211111111112222-211121222222211111311111111-1111111111--112221311211111111-131111111221-1111---1-111111311------------------111--11-111211111211112211111111111111111111111111111111111122-112222223222222332112213222122331111111112-1111111111111112111-2121124121221111-11324111111-----11------------------------111111111122-212222222-2121111---121--21221111111211-6522--21111111-----223421111311122222221222-23222223212-422222323343322111111231112111111111111-111-----------------------------12111112212111111-------111111121-13232-----1-111221132--111---1-------11111-11121---1--111111111123311111213112121111121111111111111111111112111111111111112211211111---1111------22221212222232322-2222222222232222222242111111111111111111111122222221-322222222222--1111111-11--1132111112-1111111211111111111211111132121231121111111111111111111111111111111111211111111111111------------------------------------2112222222121 ----12--21--2213433233131312222332321333232212212234451232212122112111121112212213431311-35242223442211222-1227221111-----1112-31291-121-11-41111-1--11--211-12-----11-122-1-131312V1111232173232243653 ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- STR:NPRED 390 STR:RPRED 99.7 SQ:SECSTR ccEEEEcccccHHHHHHHcHHHHHHHHTTTEEEEEEcccccccHHHHHTccEEEEcccccTTccHHHHHHHTcEEEccccTTHHHHHHHHHHHHHHHHTTHHHHHHHHHTTGGGGcccccccccTccccccccTTccEEEEcccHHHHHHHHHHHTTTccEEEEcccccTTcccEHHTTTEEEccHHHHHHTccEEEEcccccGGGTTcccHHHHHHHcTTcEEEEcccGGGccHHHHHHHHHHTcccEEEEcccTTTGGGcTTEEEccccTTccHHHHHHHHHHHHHHHHHHHHTcccccccccccHHHccccTTTHHHHHHHHHHHHHHHHHccccHHHHHTGGGTcTTcEEcccEEEETTcccccEEEcccccccccccccEEEEEc# PSIPRED ccccccccccccccccccccHHHHHHHcccccEEEEcccccccHHHccccEEEEEcccccccccHHHHHHcccEEEEcccccHHHHHHHHHHHHHHHHHcHHHHHHHHHccccHHHHcccccccccccccccccccEEEEEcccHHHHHHHHHHHHcccEEEEEEcccccccHHHccccEEEEccHHHHHHHccEEEEEccccHHHHccccHHHHHHccccEEEEEccccccccHHHHHHHHHcccEEEEEEccccHHHHccccEEEccccccccHHHHHHHHHHHHHHHHHHHHcccccccccHHHccHHHHHHHccHHHHHHHHHHHHHHHHHHHHHHccccHHHHHHcccccEEEEEEEEEccccccHHHHHHHHHccccEEEEEEEc //