KEGG   ORTHOLOGY: K05597
Entry
K05597                      KO                                     
Symbol
aspQ, ansB, ansA
Name
glutamin-(asparagin-)ase [EC:3.5.1.38]
Pathway
map00220  Arginine biosynthesis
map00250  Alanine, aspartate and glutamate metabolism
map00470  D-Amino acid metabolism
map01100  Metabolic pathways
map01110  Biosynthesis of secondary metabolites
map02020  Two-component system
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09105 Amino acid metabolism
   00250 Alanine, aspartate and glutamate metabolism
    K05597  aspQ, ansB, ansA; glutamin-(asparagin-)ase
   00220 Arginine biosynthesis
    K05597  aspQ, ansB, ansA; glutamin-(asparagin-)ase
  09106 Metabolism of other amino acids
   00470 D-Amino acid metabolism
    K05597  aspQ, ansB, ansA; glutamin-(asparagin-)ase
 09130 Environmental Information Processing
  09132 Signal transduction
   02020 Two-component system
    K05597  aspQ, ansB, ansA; glutamin-(asparagin-)ase
Enzymes [BR:ko01000]
 3. Hydrolases
  3.5  Acting on carbon-nitrogen bonds, other than peptide bonds
   3.5.1  In linear amides
    3.5.1.38  glutamin-(asparagin-)ase
     K05597  aspQ, ansB, ansA; glutamin-(asparagin-)ase
Other DBs
RN: R00256 R00485 R01579
COG: COG0252
GO: 0050417
Genes
PAE: PA1337(ansB)
PAEV: N297_1377(ansB)
PAEI: N296_1377(ansB)
PAU: PA14_46970(ansB)
PAP: PSPA7_4048(ansB)
PAG: PLES_38441(ansB)
PAF: PAM18_3565(ansB)
PNC: NCGM2_2225(ansB)
PAEB: NCGM1900_5234(ansB)
PDK: PADK2_18955
PAEP: PA1S_19220
PAEM: U769_19065
PAEL: T223_19670
PAEU: BN889_01444(ansB)
PAEG: AI22_15380
PAEC: M802_1374(ansB)
PAEO: M801_1376(ansB)
PPU: PP_2453(ansB)
PPF: Pput_3237
PPT: PPS_2020
PPI: YSA_00932
PPX: T1E_3434(ansA)
PPUH: B479_09975
PPUT: L483_21245
PPUN: PP4_19030(ansB)
PPUD: DW66_2273
PMON: X969_08385
PMOT: X970_08045
PFL: PFL_2099(ansB)
PPRC: PFLCHA0_c21450(ansB)
PPRO: PPC_2112(ansB)
PFS: PFLU_4161
PFC: PflA506_3470(ansB)
PFB: VO64_1240
PMAN: OU5_5665(ansB)
PFW: PF1751_v1c36680(ansB)
PEN: PSEEN1951(aspQ)
PPUU: PputUW4_03404(ansB)
PSEM: TO66_10680
PSEC: CCOS191_2092(ansB)
PSOS: POS17_2054(ansB)
PANR: A7J50_3841
PSIL: PMA3_09280
PDW: BV82_3721
PSEP: C4K39_2145
PTAE: NCTC10697_02838(ansB_2)
ACB: A1S_1466
ABM: ABSDF2183(aspQ)
ABY: ABAYE2188(aspQ)
ABN: AB57_1697
ABB: ABBFA_01996(ansB)
ABX: ABK1_1959
ABH: M3Q_1853
ABAD: ABD1_14640(aspQ)
ABAZ: P795_9890
ABAU: IX87_02900
ABAA: IX88_09280
ACC: BDGL_000847(aspQ)
ACI: ACIAD2088(aspQ)
AGU: AS4_18910(aspQ)
AUG: URS_2403
REH: H16_A1910(ansA)
CNC: CNE_1c18890(ansB2)
RME: Rmet_1583(ansB)
CTI: RALTA_A1603(ansB1)
CGD: CR3_4545(aspQ)
BMUL: NP80_1014(ansB)
BGO: BM43_2101(ansB)
BGP: BGL_1c06540(ansB1)
BXE: Bxe_B2492
BXB: DR64_4819
HYF: DTO96_101665(ansB_2)
POL: Bpro_4206
PNA: Pnap_0442
AAV: Aave_4182
AJS: Ajs_3863
AAA: Acav_4052
ACRA: BSY15_2021(ansB)
DAC: Daci_0564
VPD: VAPA_1c49020(ansB)
CTES: O987_02085
PBH: AAW51_1003(aspQ)
MPT: Mpe_A1913
HSE: Hsero_1444(ansB)
LCH: Lcho_2689
APET: ToN1_12480(ansB)
AZO: azo0438(ansB2)
AOA: dqs_0449
AZA: AZKH_3046(ansB2)
DTR: RSDT_0924(ansB)
MET: M446_5042
MNO: Mnod_5349
MOR: MOC_3938
MAQU: Maq22A_c08785(ansB)
MIND: mvi_32290(ansB)
SECH: B18_18425
 » show all
Reference
  Authors
Huser A, Kloppner U, Rohm KH
  Title
Cloning, sequence analysis, and expression of ansB from Pseudomonas fluorescens, encoding periplasmic glutaminase/asparaginase.
  Journal
FEMS Microbiol Lett 178:327-35 (1999)
DOI:10.1111/j.1574-6968.1999.tb08695.x
LinkDB

KEGG   ENZYME: 3.5.1.38
Entry
EC 3.5.1.38                 Enzyme                                 
Name
glutamin-(asparagin-)ase;
glutaminase-asparaginase;
ansB (gene name);
L-asparagine/L-glutamine amidohydrolase;
L-ASNase/L-GLNase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
Sysname
L-glutamine(L-asparagine) amidohydrolase
Reaction(IUBMB)
(1) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256];
(2) L-asparagine + H2O = L-aspartate + NH3 [RN:R00485]
Reaction(KEGG)
R00256 R00485;
(other) R01579 R06134
Substrate
L-glutamine [CPD:C00064];
H2O [CPD:C00001];
L-asparagine [CPD:C00152]
Product
L-glutamate [CPD:C00025];
NH3 [CPD:C00014];
L-aspartate [CPD:C00049]
Comment
The enzyme from the bacterium Achromobacter hydrolyses L-asparagine at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly. cf. EC 3.5.1.2, glutaminase and EC 3.5.1.1, asparaginase.
History
EC 3.5.1.38 created 1976
Pathway
ec00220  Arginine biosynthesis
ec00250  Alanine, aspartate and glutamate metabolism
ec00470  D-Amino acid metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K05597  glutamin-(asparagin-)ase
Genes
PAEPA1337(ansB)
PAEVN297_1377(ansB)
PAEIN296_1377(ansB)
PAUPA14_46970(ansB)
PAPPSPA7_4048(ansB)
PAGPLES_38441(ansB)
PAFPAM18_3565(ansB)
PNCNCGM2_2225(ansB)
PAEBNCGM1900_5234(ansB)
PDKPADK2_18955
PSGG655_18480
PRPM062_07255
PAEPPA1S_19220
PAERPA1R_gp4945
PAEMU769_19065
PAELT223_19670
PAESSCV20265_4073
PAEUBN889_01444(ansB)
PAEGAI22_15380
PAECM802_1374(ansB)
PAEOM801_1376(ansB)
PPUPP_2453(ansB)
PPFPput_3237
PPGPputGB1_3493
PPWPputW619_1955
PPTPPS_2020
PPBPPUBIRD1_3225
PPIYSA_00932
PPXT1E_3434(ansA)
PPUHB479_09975
PPUTL483_21245
PPUNPP4_19030(ansB)
PPUDDW66_2273
PMONX969_08385
PMOTX970_08045
PMOSO165_012770
PPJRK21_03012
PMOLCLJ08_23235
PFLPFL_2099(ansB)
PPRCPFLCHA0_c21450(ansB)
PPROPPC_2112(ansB)
PFNHZ99_07380
PFOPfl01_1917
PFSPFLU_4161
PFCPflA506_3470(ansB)
PPZH045_12070
PFBVO64_1240
PMANOU5_5665(ansB)
PTVAA957_24170
PVRPverR02_21410
PAZOAYR47_27360
POIBOP93_16805
PRXHRH33_18005
PFWPF1751_v1c36680(ansB)
PFFPFLUOLIPICF717940
PFXA7318_17450
PENPSEEN1951(aspQ)
PBAPSEBR_a2109 PSEBR_a744
PBCCD58_10640
PPUUPputUW4_03404(ansB)
PSVPVLB_15760
PSKU771_21775
PCHEY04_09895
PCZPCL1606_39600
PCPJM49_20000
PFZAV641_14720
PLQAA042_01470
PALKPSAKL28_19380
PSWLK03_16270
PPVNJ69_05435
PSEMTO66_10680
PSECCCOS191_2092(ansB)
PPSYAOC04_11755
PSOSPOS17_2054(ansB)
PKRAYO71_12555
PFKPFAS1_21525
PANRA7J50_3841
PSILPMA3_09280
PYMAK972_3826
PKEDLD99_10450
PUMHGP31_11100
PPSHG5J76_18175
PGYAWU82_02625
PATAJWU58_17720
PDWBV82_3721
PZEHU754_019400
PMOEHV782_010850
PSEPC4K39_2145
PTRTHU722_0019275
PXAKSS93_19540
PSAMHU731_005840
PTZHU718_010935
PQIKH389_17985
PSHHHU773_018315
PXNHU772_010615
PHVHU739_007940
PPRGHU725_013390
PASGKSS96_19140
PFAKKSS94_17280
PMUYKSS95_13400
PMAMKSS90_16255
PAZEKSS91_09885
PORYEJA05_18500
PTKEXN22_17680
PIEHU724_010745
PWYHU734_010800
PTAENCTC10697_02838(ansB_2)
AVNAvin_07280
AVLAvCA_07280
AVDAvCA6_07280
ACXAchr_33940
ACBA1S_1466
ABMABSDF2183(aspQ)
ABYABAYE2188(aspQ)
ABCACICU_01504
ABNAB57_1697
ABBABBFA_01996(ansB)
ABXABK1_1959
ABZABZJ_01665
ABRABTJ_02205
ABDABTW07_1665
ABHM3Q_1853
ABADABD1_14640(aspQ)
ABJBJAB07104_02254
ABABBJAB0715_01686
ABAJBJAB0868_01620
ABAZP795_9890
ABKLX00_07445
ABAUIX87_02900
ABAAIX88_09280
ABWBL01_02660
ABALABLAC_22980
ACCBDGL_000847(aspQ)
ANORR32_10605
ALCOTEC02_10815
ACALBUM88_07695
ASEII8T81_11255
ACDAOLE_11355
ACIACIAD2088(aspQ)
ATTAMQ28_09070
AEIAOY20_12600
AJORZ95_08805
ACWA0J50_10115
ACVAMD27_06455
AHLAHTJS_08975
AJNBVL33_11525
ASOLBEN76_06565
ALABFG52_08885
ADVDJ533_12280
ARJDOM24_13475
AWUBEN71_12000
AGUAS4_18910(aspQ)
AUGURS_2403
ABERBSR55_09015
ATNFM020_08250
ALJG8D99_09425
ASHAG8E00_06805
MBAHHYN46_08425
HAAA5892_07125
VFFVITFI_CDS3260
RPJN234_11060
REHH16_A1910(ansA)
CNCCNE_1c18890(ansB2)
CUHBJN34_10105
REUReut_A1812
RMERmet_1583(ansB)
CTIRALTA_A1603(ansB1)
CBWRR42_s1098
CGDCR3_4545(aspQ)
CCUPBKK81_10095
CUPBKK80_10540
CUUBKK79_02570
CPAUEHF44_13380
COXE0W60_19255 E0W60_32055
BMULNP80_1014(ansB)
BGDbgla_1g07120
BGOBM43_2101(ansB)
BGPBGL_1c06540(ansB1)
BPLAbpln_1g06460
BUMAXG89_12855
BUIAX768_06655
BXEBxe_B2492
BXBDR64_4819
BPYBphyt_4228
PSPWBJG93_31510
PCAFDSC91_000094
HYFDTO96_101665(ansB_2)
CARIFNU76_07130
PACRFXN63_16035
RHYRD110_23305
POLBpro_4206
PNAPnap_0442
POSDT070_09140
POOF7R28_00275
AAVAave_4182
AJSAjs_3863
AAAAcav_4052
ACKC380_03010
ACRABSY15_2021(ansB)
ACIOEAG14_18810
AMONH9L24_18175
AANTHUK68_17505
ARADKI609_03230
DACDaci_0564
DELDelCs14_0508
DTSBI380_24470
DHKBO996_00440
DLAI6G47_24845
VAPVapar_4748
VPEVarpa_5398
VPDVAPA_1c49020(ansB)
VAAAX767_13165
VBOCKY39_29475
VAMC4F17_22310
CTTCtCNB1_0406
CTESO987_02085
CSERCCO03_11225
CAQTKAQ61_18045
CODOLAD35_18455
OTOADJ79_11650
OTKC6570_11915 C6570_15760
DIHG7047_27185
DAERH9K75_15760
DRGH9K76_22610
DIADtpsy_3136
MELMC7H73_03415
PBHAAW51_1003(aspQ)
MPTMpe_A1913
METPC1M51_18050
HSEHsero_1444(ansB)
HSZACP92_07245
HHTF506_08165
HEEhmeg3_17630
HHFE2K99_07295
HFRG5S34_07620
LCHLcho_2689
RGUA4W93_04140
AONDEH84_13150
XYKGT347_15600
ARESIWH25_18190
APETToN1_12480(ansB)
QAUKI612_08430
FLEKI610_03125
AZOazo0438(ansB2)
AOAdqs_0449
AZAAZKH_3046(ansB2)
AZIAzCIB_3394
AZDCDA09_06580
AZRCJ010_02915
THKCCZ27_16325
APPCAP2UW1_1093
DTRRSDT_0924(ansB)
MRDMrad2831_3427
METM446_5042
MNOMnod_5349
MORMOC_3938
MAQUMaq22A_c08785(ansB)
MPHYMCBMB27_02915
MEEDA075_09085
METXA3862_14320
METIDK427_14455
MMESMMSR116_12420
MTEADK419_23660
MINDmvi_32290(ansB)
CMETK6K41_27075
SECHB18_18425
PARHI5S86_10635
 » show all
Reference
1  [PMID:5017769]
  Authors
Roberts J, Holcenberg JS, Dolowy WC.
  Title
Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity.
  Journal
J Biol Chem 247:84-90 (1972)
Reference
2  [PMID:3379033]
  Authors
Tanaka S, Robinson EA, Appella E, Miller M, Ammon HL, Roberts J, Weber IT, Wlodawer A
  Title
Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase  from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi.
  Journal
J Biol Chem 263:8583-91 (1988)
Reference
3  [PMID:8068664]
  Authors
Lubkowski J, Wlodawer A, Ammon HL, Copeland TD, Swain AL
  Title
Structural characterization of Pseudomonas 7A glutaminase-asparaginase.
  Journal
Biochemistry 33:10257-65 (1994)
DOI:10.1021/bi00200a005
  Sequence
Reference
4  [PMID:10684596]
  Authors
Ortlund E, Lacount MW, Lewinski K, Lebioda L
  Title
Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu.
  Journal
Biochemistry 39:1199-204 (2000)
DOI:10.1021/bi991797d
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.38
IUBMB Enzyme Nomenclature: 3.5.1.38
ExPASy - ENZYME nomenclature database: 3.5.1.38
BRENDA, the Enzyme Database: 3.5.1.38
CAS: 39335-03-0
LinkDB

KEGG   REACTION: R00485
Entry
R00485                      Reaction                               
Name
L-asparagine amidohydrolase
Definition
L-Asparagine + H2O <=> L-Aspartate + Ammonia
Equation
Reaction class
RC00010  C00049_C00152
RC02798  C00014_C00152
Enzyme
3.5.1.1         3.5.1.38        3.5.5.4
Pathway
rn00250  Alanine, aspartate and glutamate metabolism
rn00460  Cyanoamino acid metabolism
rn01100  Metabolic pathways
rn01110  Biosynthesis of secondary metabolites
Orthology
K01424  L-asparaginase [EC:3.5.1.1]
K05597  glutamin-(asparagin-)ase [EC:3.5.1.38]
K13051  L-asparaginase / beta-aspartyl-peptidase [EC:3.5.1.1 3.4.19.5]
Other DBs
RHEA: 21019
LinkDB

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