KEGG   ENZYME: 2.6.1.92Help
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
BRITE hierarchy
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)
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
Orthology
K15895  UDP-4-amino-4,6-dideoxy-L-N-acetyl-beta-L-altrosamine transaminase
Genes
HPY: HP0366
HEO: C694_01855
HPJ: jhp_1015
HPA: HPAG1_1028
HPS: HPSH_05585
HHP: HPSH112_05385
HHQ: HPSH169_05370
HHR: HPSH417_05135
HPG: HPG27_1031
HPP: HPP12_1055
HPB: HELPY_1059(pseC)
HPL: HPB8_414(spsC)
HPO: HMPREF4655_21279(pseC)
HPQ: hp2017_1041(pseC)
HPW: hp2018_1045(pseC)
HPZ: HPKB_1017
HPX: HMPREF0462_1102(pseC)
HPYS: HPSA20_1156(pseC)
HPD: KHP_0990
HEY: MWE_1267
HPYR: K747_11805
HPYI: K750_07040
HPYU: K751_02210
HPYM: K749_00295
HEB: U063_1403
HEZ: U064_1408
HHE: HH_0197
HAC: Hac_0518
HMS: HMU02370
HCE: HCW_04930
HCM: HCD_07475
HCP: HCN_1534
WSU: WS1076
SUA: Saut_0142
SULR: B649_00710
CJE: Cj1294(pseC)
CJB: BN148_1294(pseC)
CJU: C8J_1237
CJI: CJSA_1232(pseC)
CJM: CJM1_1276(pseC)
CJS: CJS3_1391(pseC)
CJEJ: N564_01312
CJEU: N565_01349
CJEN: N755_01344
CJEI: N135_01382
CJER: H730_07420
CJV: MTVDSCj20_1300(pseC)
CJY: QZ67_01429(pseC)
CJQ: UC78_1246(pseC)
CJR: CJE1486
CFT: CFF04554_1576(pseC)
CFV: CFVI03293_1598(pseC)
CFX: CFV97608_1700(pseC)
CFZ: CSG_17040
CAMP: CFT03427_1526(pseC)
CCV: CCV52592_0561(pseC)
CLA: Cla_1299
CLR: UPTC16701_1282(pseC)
CLM: UPTC16712_1301(pseC)
CLQ: UPTC4110_1285(pseC)
CLN: UPTC3659_1522(pseC)
CLL: CONCH_1252(pseC)
CCQ: N149_1255
CCF: YSQ_02390
CCY: YSS_07025
CCOI: YSU_02415
CCOF: VC76_06495(pseC)
CCOO: ATE51_00976(pseC)
CAJ: CIG1485E_1519(pseC)
CIS: CINS_1262(pseC)
CVO: CVOL_1278(pseC)
CPEL: CPEL_1408(pseC)
CAMR: CAQ16704_1311(pseC)
CSM: CSUB8521_1488(pseC)
CSF: CSUB8523_1584(pseC)
CHYO: CHH_1613(pseC)
CHV: CHELV3228_0314(pseC)
CSPF: CSF_1305(pseC)
CPIN: CPIN18020_0091(pseC)
CCUN: CCUN_0612(pseC)
CLX: CLAN_1519(pseC)
CAVI: CAV_1206(pseC)
CHW: A2J15_000550(pseC)
SDL: Sdel_2209
SMUL: SMUL_3173(pseC)
SHAL: SHALO_2908
SULJ: SJPD1_2793
 » show all
Taxonomy
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:HP0366] [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:HP0366]
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

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