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Candidatus Pelagibacter ubique HTCC1062 (pubi0)
Gene : hisD
DDBJ      :hisD         Histidinol dehydrogenase
Swiss-Prot:HISX1_PELUB  RecName: Full=Histidinol dehydrogenase 1;         Short=HDH 1;         EC=1.1.1.23;

Homologs  Archaea  55/68 : Bacteria  713/915 : Eukaryota  120/199 : Viruses  0/175   --->[See Alignment]
c.82.1
:428 amino acids
:SECSTR
:PSIPRED
:DISOPRED
:BLT:PDB   48->425 1kaeA PDBj 2e-53 36.2 %
:RPS:PDB   172->338 2bvcA PDBj 5e-21 12.1 %
:RPS:SCOP  68->427 1k75A  c.82.1.2 * 5e-35 35.4 %
:HMM:SCOP  2->430 1k75A_ c.82.1.2 * 1e-65 22.8 %
:RPS:PFM   48->425 PF00815 * Histidinol_dh 2e-91 47.5 %
:HMM:PFM   20->425 PF00815 * Histidinol_dh 9.2e-138 41.8 404/413  
:BLT:SWISS 1->428 HISX1_PELUB 0.0 100.0 %
:PROS 26->41|PS00012|PHOSPHOPANTETHEINE
:PROS 226->259|PS00611|HISOL_DEHYDROGENASE
:SEG

SeqInfo AminoSeq See neighboring genes
Links GIB DAD Abbreviations Back to title page
GT:ID AAZ21297.1 GT:GENE hisD GT:PRODUCT Histidinol dehydrogenase GT:DATABASE GIB00256CH01 GT:ORG pubi0 GB:ACCESSION GIB00256CH01 GB:LOCATION 465046..466332 GB:FROM 465046 GB:TO 466332 GB:DIRECTION + GB:GENE hisD GB:PRODUCT Histidinol dehydrogenase GB:PROTEIN_ID AAZ21297.1 GB:DB_XREF GI:71062294 GB:GENE:GENE hisD LENGTH 428 SQ:AASEQ MIKILDSKNKNFDKTLDALLSKRKNKVQLNSVSVIKIIKDVKKNGDKAILKYEKRFNKNSIIAPSIKQINRAIQSLDQKVKKAIDLAYDRIYKFHSLQKFKNISYTDKLKNKLEYKYVPIESVAIYVPGSTASYPSSVLMNAVPAIVAGVKRLVMVNPGQKGKQNPAVLYAAKKCKIKEIYSIGGPSAIAAVAYGTKKIKKVDKIIGPGNSYVAAAKKEVFGDVGIEGMIAGPSEVTIVCDKFSNPEWIASDLIGQAEHDNLAQCILISKDKSIIKKVNYEIINQLKELPRAVIAKNSLLNNGILIYMPSDQKIINTVNKIAPEHLELNTKNYKKVVSKIKNAGSICLGKYAVMAMTDYNVGSNHVLPTNSSARYSSGVSVNEFYKRISYINLSKKGIETLGPSVITLANYEGLVGHAKSVEKRIRRK GT:EXON 1|1-428:0| SW:ID HISX1_PELUB SW:DE RecName: Full=Histidinol dehydrogenase 1; Short=HDH 1; EC=1.1.1.23; SW:GN Name=hisD1; OrderedLocusNames=SAR11_0475; SW:KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis;Metal-binding; NAD; Oxidoreductase; Zinc. SW:EXACT T SW:FUNC + BL:SWS:NREP 1 BL:SWS:REP 1->428|HISX1_PELUB|0.0|100.0|428/428| GO:SWS:NREP 5 GO:SWS GO:0008652|"GO:cellular amino acid biosynthetic process"|Amino-acid biosynthesis| GO:SWS GO:0000105|"GO:histidine biosynthetic process"|Histidine biosynthesis| GO:SWS GO:0046872|"GO:metal ion binding"|Metal-binding| GO:SWS GO:0016491|"GO:oxidoreductase activity"|Oxidoreductase| GO:SWS GO:0055114|"GO:oxidation reduction"|Oxidoreductase| PROS 26->41|PS00012|PHOSPHOPANTETHEINE|PDOC00012| PROS 226->259|PS00611|HISOL_DEHYDROGENASE|PDOC00534| SEG 30->47|nsvsvikiikdvkkngdk| SEG 266->277|iliskdksiikk| BL:PDB:NREP 1 BL:PDB:REP 48->425|1kaeA|2e-53|36.2|370/427| RP:PDB:NREP 1 RP:PDB:REP 172->338|2bvcA|5e-21|12.1|157/475| RP:PFM:NREP 1 RP:PFM:REP 48->425|PF00815|2e-91|47.5|377/412|Histidinol_dh| HM:PFM:NREP 1 HM:PFM:REP 20->425|PF00815|9.2e-138|41.8|404/413|Histidinol_dh| GO:PFM:NREP 4 GO:PFM GO:0000105|"GO:histidine biosynthetic process"|PF00815|IPR012131| GO:PFM GO:0004399|"GO:histidinol dehydrogenase activity"|PF00815|IPR012131| GO:PFM GO:0008270|"GO:zinc ion binding"|PF00815|IPR012131| GO:PFM GO:0051287|"GO:NAD or NADH binding"|PF00815|IPR012131| RP:SCP:NREP 1 RP:SCP:REP 68->427|1k75A|5e-35|35.4|356/431|c.82.1.2| HM:SCP:REP 2->430|1k75A_|1e-65|22.8|421/0|c.82.1.2|1/1|ALDH-like| OP:NHOMO 987 OP:NHOMOORG 888 OP:PATTERN ---1--1111111111-1111111111111111111111111111111111111-1-111-1----11 1111111111211111111-11111311111111111122111121111111112111--111111211111111111--11111111111111-----1-111111111---------------111111111111111111111222122211111111111211221111111111111111111111111111111111111111211111111111111111111111-11111111111111111-1----11-1---11--11----1-111-------111------------------------1----1----11-1111111-1-1111111---1-1--1111111112111111111--11111111-----111111111111111111111112111111211231-2111123212421111133321223131111111111111111-----------------------------21211111111122121111111112111111112122111111111111111121111111111111111111111-1211111111111-1111111111111111111111111111-1-------11111111111112111111111111111111111111--111111111111111111111111111-1111111111111111111111111111111111111111111111111111-11111111111111-1-----111111111111111-1111---1-11111111111111111121111111111--------111111111121111111111111111111111111111--------------------------------------1--1-111111 ------1-----11111212221232111111111111111111111111122232111111111111-1111111111111111111-11111111111111111-15-------------------------------------------------1----------------111181111121332231121111 ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- STR:NPRED 373 STR:RPRED 87.1 SQ:SECSTR ###############################################HHHHHTTcccccccccccHHHHHHHHHHccHHHHHHH#HHHHHHHHHHHTTccccEEEEEETTEEEEEEEEEccEEEEEccccccccTHHHHH#HHHHHHHTccEEEEEEcccccHH###HHHHGGccHHHHHHHHHHHHHHHHHHHHHcccTTHHHHccTTccccccccEEETcTccEHEEccccccTTccccccccHHHHHHHHHHHHHHHHHTTccccccccccGGGccHHHHHTccccccHHHHHHcHHHccHHHHHHHcHcHHHHGGGcccHHHHHHHHHHHTcccGcEEccccccccccccTTccccccHHHHTcHHHHHHTcTTccEEEEcHHHHTccccHHHHHHGGGGTTcHHHHTTcHHHHHHHHHHH### DISOP:02AL 20-28, 427-428| PSIPRED cccEEEcccccHHHHHHHHHccccccHHHHHHHHHHHHHHHHHHHHHHHHHHHHHccccccccccHHHHHHHHHHccHHHHHHHHHHHHHHHHHHHHHcccccEEEEcccEEEEEEEEEEEHEEEEccccccHHHHHHHHHHHHHEEEcccEEEEEEccccccccHHHHHHHHHHHHHHHHHHccHHHHHHHHHccccccccEEEEccccHHHHHHHHHHcccccccccccccEEEEEEEcccccHHHHHHHHHHHHHcccccEEEEEEccHHHHHHHHHHHHHHHHHccHHHHHHHHHHcccEEEEEccHHHHHHHHHHHcHHHHHHHHHHHHHHHHHHHHHHHHEEcccccHHHccccccccccccccccHHHcccccHHHHccEEEEEEEcHHHHHHHHHHHHHHHHHcccHHHHHHHHHHHHcc //