KEGG   ENZYME: 2.6.1.92
Entry
EC 2.6.1.92                 Enzyme                                 
Name
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase;
PseC;
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine:2-oxoglutarate aminotransferase;
UDP-beta-L-threo-pentapyranos-4-ulose transaminase;
UDP-4-dehydro-6-deoxy-D-glucose transaminase
Class
Transferases;
Transferring nitrogenous groups;
Transaminases
Sysname
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine:2-oxoglutarate transaminase
Reaction(IUBMB)
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + L-glutamate [RN:R09825]
Reaction(KEGG)
R09825
Substrate
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine [CPD:C19961];
2-oxoglutarate [CPD:C00026]
Product
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose [CPD:C19823];
L-glutamate [CPD:C00025]
Comment
A pyridoxal 5'-phosphate protein. The enzyme transfers the primary amino group of L-glutamate to C-4'' of UDP-4-dehydro sugars, forming a C-N bond in a stereo configuration opposite to that of UDP. The enzyme from the bacterium Bacillus cereus has been shown to act on UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose, UDP-beta-L-threo-pentapyranos-4-ulose, UDP-4-dehydro-6-deoxy-D-glucose, and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose. cf. EC 2.6.1.34, UDP-N-acetylbacillosamine transaminase, which catalyses a similar reaction, but forms the C-N bond in the same stereo configuration as that of UDP.
History
EC 2.6.1.92 created 2011, modified 2018
Pathway
ec00520  Amino sugar and nucleotide sugar metabolism
ec00541  O-Antigen nucleotide sugar biosynthesis
ec01100  Metabolic pathways
Orthology
K15895  UDP-4-amino-4,6-dideoxy-L-N-acetyl-beta-L-altrosamine transaminase
Genes
HPYHP_0366
HEOC694_01855
HPJjhp_1015
HPAHPAG1_1028
HPSHPSH_05585
HHPHPSH112_05385
HHQHPSH169_05370
HHRHPSH417_05135
HPGHPG27_1031
HPPHPP12_1055
HPBHELPY_1059(pseC)
HPLHPB8_414(spsC)
HPCHPPC_05285
HCAHPPC18_05385
HPMHPSJM_05365
HPEHPELS_01240
HPOHMPREF4655_21279(pseC)
HPIhp908_1081
HPQhp2017_1041(pseC)
HPWhp2018_1045(pseC)
HPUHPCU_05515
HEFHPF16_1032
HPFHPF30_0299
HEQHPF32_1026
HEXHPF57_1051
HPTHPSAT_05195
HPZHPKB_1017
HPVHPV225_1105
HPXHMPREF0462_1102(pseC)
HENHPSNT_05400
HPHHPLT_05385
HEGHPGAM_05595
HPNHPIN_05370
HEPHPPN120_05270
HEUHPPN135_05560
HESHPSA_05280
HPYSHPSA20_1156(pseC)
HCNHPB14_05085
HPDKHP_0990
HEYMWE_1267
HERC695_01855
HEIC730_01855
HPYAHPAKL117_05090
HPYKHPAKL86_02535
HPYOHPOK113_1050
HPYLHPOK310_0986
HPYBHPOKI102_05705
HPYCHPOKI112_05740
HPYDHPOKI128_05125
HPYEHPOKI154_05410
HPYFHPOKI422_05730
HPYGHPOKI673_05395
HPYHHPOKI828_05405
HPYJHPOKI898_05715
HPYRK747_11805
HPYIK750_07040
HPYUK751_02210
HPYMK749_00295
HEMK748_06855
HEBU063_1403
HEZU064_1408
HHEHH_0197
HACHac_0518
HMSHMU02370
HFEHFELIS_14250
HBIHBZC1_14300
HCEHCW_04930
HCMHCD_07475
HCPHCN_1534
HCBHCBAA847_1760
HHMBN341_11460
HTYBN2458_PEG1438
HBLXJ32_06750
HETBBW65_06955
HCLNCTC13205_01305(arnB_2)
HSHNHP194022_08810(pseC)
WSUWS1076
SUASaut_0142
SKUSulku_0151
SULRB649_00710
CJECj1294(pseC)
CJBBN148_1294(pseC)
CJJCJJ81176_1311
CJUC8J_1237
CJNICDCCJ07001_1242
CJICJSA_1232(pseC)
CJMCJM1_1276(pseC)
CJSCJS3_1391(pseC)
CJPA911_06285
CJEJN564_01312
CJEUN565_01349
CJENN755_01344
CJEIN135_01382
CJERH730_07420
CJVMTVDSCj20_1300(pseC)
CJYQZ67_01429(pseC)
CJQUC78_1246(pseC)
CJLPJ17_06860
CJWPJ18_06670
CJRCJE1486
CJDJJD26997_0428
CJZM635_02165
CJXBN867_12870
CFFCFF8240_1567
CFTCFF04554_1576(pseC)
CFVCFVI03293_1598(pseC)
CFXCFV97608_1700(pseC)
CFZCSG_17040
CAMPCFT03427_1526(pseC)
CFPCR44_07740
CCVCCV52592_0561(pseC)
CLACLA_1299(pseC)
CLRUPTC16701_1282(pseC)
CLMUPTC16712_1301(pseC)
CLQUPTC4110_1285(pseC)
CLNUPTC3659_1522(pseC)
CLLCONCH_1252(pseC)
CCOLBN865_08350c
CCCG157_02350
CCQN149_1255(pseC)
CCFYSQ_02390
CCYYSS_07025
CCOIYSU_02415
CCOFVC76_06495(pseC)
CCOOATE51_00976(pseC)
CAJCIG1485E_1519(pseC)
CISCINS_1262(pseC)
CVOCVOL_1278(pseC)
CPELCPEL_1408(pseC)
CAMRCAQ16704_1311(pseC)
CSMCSUB8521_1488(pseC)
CSFCSUB8523_1584(pseC)
CHYOCHH_1613(pseC)
CHVCHELV3228_0314(pseC)
CSPFCSF_1305(pseC)
CPINCPIN18020_0091(pseC)
CCUNCCUN_0612(pseC)
CLXCLAN_1519(pseC)
CAVICAV_1206(pseC)
CHWA2J15_000550(pseC)
CAMZCVIC12175_0290(pseC)
CAMYCSUIS_0257(pseC)
COJCORN_1371(pseC)
CUXCUP3940_1333(pseC)
CRXCRECT_0234(pseC)
CARMCARM_1335(pseC)
CMUCCMCT_0212(pseC)
CSHOCSHOW_1832(pseC)
CINFCINF_1743(pseC)
CNVCNZW441b_1260(pseC)
SDLSdel_2209
SBASulba_2443
SMULSMUL_3173(pseC)
SHALSHALO_2908
SULSSdiek1_2897
SULJSJPD1_2793
SULTFA592_06765(pseC)
NISNIS_1650
 » show all
Reference
1  [PMID:16286454]
  Authors
Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM
  Title
Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways.
  Journal
J Biol Chem 281:723-32 (2006)
DOI:10.1074/jbc.M511021200
  Sequence
[hpy:HP_0366] [cje:Cj1294]
Reference
2  [PMID:16421095]
  Authors
Schoenhofen IC, Lunin VV, Julien JP, Li Y, Ajamian E, Matte A, Cygler M, Brisson JR, Aubry A, Logan SM, Bhatia S, Wakarchuk WW, Young NM
  Title
Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori.
  Journal
J Biol Chem 281:8907-16 (2006)
DOI:10.1074/jbc.M512987200
  Sequence
[hpy:HP_0366]
Reference
3  [PMID:23458065]
  Authors
Mostafavi AZ, Troutman JM
  Title
Biosynthetic assembly of the Bacteroides fragilis capsular polysaccharide A precursor bactoprenyl diphosphate-linked acetamido-4-amino-6-deoxygalactopyranose.
  Journal
Biochemistry 52:1939-49 (2013)
DOI:10.1021/bi400126w
Reference
4  [PMID:25368324]
  Authors
Hwang S, Li Z, Bar-Peled Y, Aronov A, Ericson J, Bar-Peled M
  Title
The biosynthesis of UDP-d-FucNAc-4N-(2)-oxoglutarate (UDP-Yelosamine) in Bacillus cereus ATCC 14579: Pat and Pyl, an aminotransferase and an ATP-dependent Grasp protein that ligates 2-oxoglutarate to UDP-4-amino-sugars.
  Journal
J Biol Chem 289:35620-32 (2014)
DOI:10.1074/jbc.M114.614917
Other DBs
ExplorEnz - The Enzyme Database: 2.6.1.92
IUBMB Enzyme Nomenclature: 2.6.1.92
ExPASy - ENZYME nomenclature database: 2.6.1.92
BRENDA, the Enzyme Database: 2.6.1.92
LinkDB

DBGET integrated database retrieval system