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Desulfotomaculum reducens MI-1 (dred0)
Gene : ABO48649.1
DDBJ      :             UDP-N-acetylglucosamine pyrophosphorylase / glucosamine-1-phosphate N-acetyltransferase
Swiss-Prot:GLMU_DESRM   RecName: Full=Bifunctional protein glmU;Includes:  RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase;           EC=2.7.7.23;  AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase;Includes:  RecName: Full=Glucosamine-1-phosphate N-acetyltransferase;           EC=2.3.1.157;

Homologs  Archaea  59/68 : Bacteria  843/915 : Eukaryota  25/199 : Viruses  1/175   --->[See Alignment]
b.81.1c.68.1
:456 amino acids
:SECSTR
:PSIPRED
:DISOPRED
:BLT:PDB   5->444 1hm9A PDBj e-114 46.8 %
:RPS:PDB   2->453 3dk5A PDBj e-117 44.5 %
:RPS:SCOP  3->251 1fwyA2  c.68.1.5 * 7e-53 42.0 %
:RPS:SCOP  252->451 1g95A1  b.81.1.4 * 5e-27 42.0 %
:HMM:SCOP  2->253 1g97A2 c.68.1.5 * 3.4e-68 40.0 %
:HMM:SCOP  248->444 2jf2A1 b.81.1.1 * 5.2e-49 39.2 %
:RPS:PFM   5->214 PF00483 * NTP_transferase 2e-23 37.7 %
:HMM:PFM   5->219 PF00483 * NTP_transferase 4.4e-22 27.4 208/248  
:HMM:PFM   198->275 PF11977 * RNase_Zc3h12a 0.00014 26.1 69/155  
:BLT:SWISS 1->456 GLMU_DESRM 0.0 100.0 %
:PROS 402->430|PS00101|HEXAPEP_TRANSFERASES
:REPEAT 2|267->311|318->362
:SEG

SeqInfo AminoSeq See neighboring genes
Links GIB DAD Abbreviations Back to title page
GT:ID ABO48649.1 GT:GENE ABO48649.1 GT:PRODUCT UDP-N-acetylglucosamine pyrophosphorylase / glucosamine-1-phosphate N-acetyltransferase GT:DATABASE GIB00494CH01 GT:ORG dred0 GB:ACCESSION GIB00494CH01 GB:LOCATION 104946..106316 GB:FROM 104946 GB:TO 106316 GB:DIRECTION + GB:PRODUCT UDP-N-acetylglucosamine pyrophosphorylase / glucosamine-1-phosphate N-acetyltransferase GB:NOTE KEGG: chy:CHY_0192 UDP-N-acetylglucosamine pyrophosphorylase TIGRFAM: UDP-N-acetylglucosamine pyrophosphorylase PFAM: 4-diphosphocytidyl-2C-methyl-D-erythritol synthase; transferase hexapeptide repeat containing protein; Nucleotidyl transferase GB:PROTEIN_ID ABO48649.1 GB:DB_XREF GI:134050678 InterPro:IPR001228 InterPro:IPR001451 InterPro:IPR005835 InterPro:IPR005882 LENGTH 456 SQ:AASEQ MELAAVILAAGKGTRMKSNLPKVLHQLCGRPMLSHVLNSVVAAGVDKTVVVAGFGAEQVTDFVGEKARVVLQREQLGTAHALLQAEGELTDYPGHLLVVCGDTPLLRAETLAKLADYHCESGAVATLLTAEMADPTGYGRVIRTTEGNVSHIVEQKDASPEELNVHEINTGVYCFKVPGLFNALKEISPANVQGEYYLTDIIQIFVQRGLTVKAVTLEDAREVQGINDRIQLSRAEVVLRHRVLEELMVQGVTIMDPENTYVDQGVKVGNDTVILPFTFLQGKTEIGSQCVLGPGSKINNCIIGDRNEIQYSVLVESKIGNDATIGPYAYLRPGTVLADHVKVGDFVEIKKSTIGHGSKIPHLSYVGDATIGEKVNVGAGTITCNYDGKKKYQTTLEDGAFIGSNTNLVAPVKVGQGAVIAAGSTITKDVPDNALGVARGRQTNLADWPKKQRKNS GT:EXON 1|1-456:0| SW:ID GLMU_DESRM SW:DE RecName: Full=Bifunctional protein glmU;Includes: RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase; EC=2.7.7.23; AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase;Includes: RecName: Full=Glucosamine-1-phosphate N-acetyltransferase; EC=2.3.1.157; SW:GN Name=glmU; OrderedLocusNames=Dred_0099; SW:KW Acyltransferase; Cell shape; Cell wall biogenesis/degradation;Complete proteome; Cytoplasm; Magnesium; Metal-binding;Multifunctional enzyme; Nucleotidyltransferase;Peptidoglycan synthesis; Repeat; Transferase. SW:EXACT T SW:FUNC + BL:SWS:NREP 1 BL:SWS:REP 1->456|GLMU_DESRM|0.0|100.0|456/456| GO:SWS:NREP 9 GO:SWS GO:0008415|"GO:acyltransferase activity"|Acyltransferase| GO:SWS GO:0008360|"GO:regulation of cell shape"|Cell shape| GO:SWS GO:0007047|"GO:cellular cell wall organization"|Cell wall biogenesis/degradation| GO:SWS GO:0005737|"GO:cytoplasm"|Cytoplasm| GO:SWS GO:0046872|"GO:metal ion binding"|Metal-binding| GO:SWS GO:0003824|"GO:catalytic activity"|Multifunctional enzyme| GO:SWS GO:0016779|"GO:nucleotidyltransferase activity"|Nucleotidyltransferase| GO:SWS GO:0009252|"GO:peptidoglycan biosynthetic process"|Peptidoglycan synthesis| GO:SWS GO:0016740|"GO:transferase activity"|Transferase| PROS 402->430|PS00101|HEXAPEP_TRANSFERASES|PDOC00094| NREPEAT 1 REPEAT 2|267->311|318->362| SEG 40->52|vvaagvdktvvva| BL:PDB:NREP 1 BL:PDB:REP 5->444|1hm9A|e-114|46.8|440/458| RP:PDB:NREP 1 RP:PDB:REP 2->453|3dk5A|e-117|44.5|425/442| RP:PFM:NREP 1 RP:PFM:REP 5->214|PF00483|2e-23|37.7|204/238|NTP_transferase| HM:PFM:NREP 2 HM:PFM:REP 5->219|PF00483|4.4e-22|27.4|208/248|NTP_transferase| HM:PFM:REP 198->275|PF11977|0.00014|26.1|69/155|RNase_Zc3h12a| GO:PFM:NREP 2 GO:PFM GO:0009058|"GO:biosynthetic process"|PF00483|IPR005835| GO:PFM GO:0016779|"GO:nucleotidyltransferase activity"|PF00483|IPR005835| RP:SCP:NREP 2 RP:SCP:REP 3->251|1fwyA2|7e-53|42.0|245/249|c.68.1.5| RP:SCP:REP 252->451|1g95A1|5e-27|42.0|200/201|b.81.1.4| HM:SCP:REP 2->253|1g97A2|3.4e-68|40.0|250/250|c.68.1.5|1/1|Nucleotide-diphospho-sugar transferases| HM:SCP:REP 248->444|2jf2A1|5.2e-49|39.2|186/0|b.81.1.1|1/1|Trimeric LpxA-like enzymes| OP:NHOMO 1210 OP:NHOMOORG 928 OP:PATTERN 221212213333333212------5553433412111111111222324323312222223111---1 1113212112221211111-1111211111121111122233331111111111111111111112233321111111111131112111-1-------1--11-11---111111111-1111-22222222223222433332242312331122111122121622221122222111122322243112111111111111111111111111112112111111113211111111111111-111111111-11111111111211111111111112222112222222222211111111111112121112222211211111111111212211111121121-2121324121212211111121111111111111111111211211111111111-111111111111111111111111211121111111111111111111111111111----------11111111111111111111111111111111111111111111111111111111111112111111112122111112111111111111111-1111211111112323222223111111111221111111111111111111111111111111111111111112111111211211-1111111-11111111111111111111-1111111111111111111111111111111111111111111111111111111111111111111111111111111111111111111111111111121111112111112111111111111111111111111111111111111111111111111111112111111----------1-------------------------1323133323--1 --------2----1----1-----------------------------------------------1---------------------------------1-------2-------------1------------------------------1----2-----11-2---1-1-211-----1221141-1------- --------------------------------------------------------------------------------------------------------------------------------------------------------------------------1---- STR:NPRED 456 STR:RPRED 100.0 SQ:SECSTR ccEEEEEEEccccGGGcccccGGGcEETTEEHHHHHHHHHHHHcccEEEEEEcccHHHHTTTTTTHHHEEEccccccHHHHHHHHHTTccTcccEEEEEEcccTTccHHHHHHHHHHHHHTTccEEEEEEccccccTcccccccTTccEEEEEcGGGccTTGGccccEEEEEEEEcHHHHHHHHHTccccccccccccTHHHHHHHHTTccEEccEEccGGGGcccccHHHHHHHHHHHHHHHHHHHHHTTcEEccGGGEEEccccEEcTTcEEcccEEEETTcEEccccEEccccEEEEEEEcTTcEEccEEEEEEEEcTTcEEcccEEEcTTEEEcTTcEEEETEEEEccEEcTTcEEEEccEEEcEEEccccccccccEEEcccccccccEEEcccccccTTcEEEcccEEcTTcEEcTTcEEcccccTTcEEcccccccccTTHHHHHcTHc DISOP:02AL 1-1,448-449,452-457| PSIPRED ccEEEEEEcccccccccccccccEEEEccEEHHHHHHHHHHHcccccEEEEEcccHHHHHHHHccccEEEEEccccccHHHHHHHHHHHccccccEEEEEcccEEEccccHHHHHHHHHHccccEEEEEEEccccccccEEEEcccccEEEEEEcccccHHHccccEEEEEEEEEcHHHHHHHHHHcccccccccHHHHHHHHHHHHcccEEEEEEEcccEEEccHHHHHHHHHHHHHHHccccccccccccEEccccccEEcccEEEccccEEcccEEEccccEEccccEEccccEEEccEEEcccEEcccEEEccEEEcccccccccEEccccEEcccccccccEEEEccEEccccEEccccEEcccEEccccEEccccEEEcccccccccEEEcccEEEccccEEEccEEEccccEEccccEEccccccccEEEEccccccHHcccccccccc //