KEGG   ENZYME: 1.5.1.51
Entry
EC 1.5.1.51                 Enzyme                                 
Name
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase;
SbnB
Class
Oxidoreductases;
Acting on the CH-NH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate:NAD+ dehydrogenase (L-2,3-diaminopropanoate-forming)
Reaction(IUBMB)
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O = 2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+ [RN:R11655]
Reaction(KEGG)
R11655
Substrate
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate [CPD:C21559];
NAD+ [CPD:C00003];
H2O [CPD:C00001]
Product
2-oxoglutarate [CPD:C00026];
L-2,3-diaminopropanoate [CPD:C03401];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.
History
EC 1.5.1.51 created 2017
Pathway
ec00997  Biosynthesis of various other secondary metabolites
ec00998  Biosynthesis of various antibiotics
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K21721  N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase
Genes
ACCBDGL_001498(ocd2)
ANORR32_07480
ACALBUM88_11500
ASEII8T81_07365(sbnB)
ACDAOLE_07115
ACWA0J50_07100
AGUAS4_16160
SDNSden_0589
CEKD0B88_14055(sbnB)
CEGD0C16_05385(sbnB)
RSORSp0418
RSLRPSI07_mp0379
RSNRSPO_m01410
RSMCMR15_mp10431
RSEF504_3906
RSYRSUY_34860(rapL_2)
RPUCDC45_19720
RSGJK151_14180(sbnB)
CNCCNE_2c14840(ocd)
CUHBJN34_08320
RMERmet_1116(ocd)
BPLAbpln_2g05020
NLCEBAPG3_006455
DBKDGMP_24730
MNOMnod_6949
MAQUMaq22A_c25430
SBDATN00_04615
BTHTH175_328p223
BBADK7T73_21445(sbnB)
PCALBV455_03923
LMACI6G82_02105(sbnB)
SCIAHUG15_04755
SAUSA0113(sbnB)
SAVSAV0117
SAWSAHV_0116
SAHSaurJH1_0108
SAJSaurJH9_0104
SAMMW0090(sbnB)
SASSAS0091
SARSAR0120
SACSACOL0101
SAXUSA300HOU_0128(ocd)
SAASAUSA300_0119
SAOSAOUHSC_00076
SAENWMN_0061(sbnB)
SADSAAV_0085
SUUM013TW_0107(sbnB)
SUVSAVC_00325
SUESAOV_0064
SUJSAA6159_00100
SUKSAA6008_00095
SUCECTR2_73
SUTSAT0131_00103
SUQHMPREF0772_10380
SUZMS7_0109
SUDST398NM01_0128
SUXSAEMRSA15_00830(sbnB)
SUWSATW20_01290(sbnB)
SUGSAPIG0128
SUFSARLGA251_00920(sbnB)
SAUASAAG_00601
SAUERSAU_000071
SAUNSAKOR_00091
SAUSSA40_0084(sbnB)
SAUUSA957_0099(sbnB)
SAUGSA268_0096(sbnB)
SAUZSAZ172_0128(sbnB)
SAUTSAI1T1_2000730
SAUJSAI2T2_1000730
SAUKSAI3T3_1000730
SAUQSAI4T8_1000730
SAUVSAI7S6_1000730
SAUWSAI5S5_1000730
SAUXSAI6T6_1000730
SAUYSAI8T7_1000730
SAUFX998_0096
SABSAB0056
SUYSA2981_0118(sbnB)
SAUBC248_0105
SAUMBN843_1190
SAUCCA347_128
SAURSABB_01723(sbnB)
SAUIAZ30_00610
SAUDCH52_05135
SAMSNI36_00505
SUHSAMSHR1132_00930
SSDSPSINT_0335
SDTSPSE_2123(sbnB)
SDPNCTC12225_02340(sbnB)
SHUSHYC_00360(sbnB)
SSCHLH95_00360
SSCZRN70_00580
SAGQEP23_09765(sbnB)
SEQOSE1039_25100
SLZB5P37_07595
SARLSAP2_02040
SSHNCTC13712_00070
SFFFOB90_07430(sbnB)
BLRBRLA_c008320
BAGRBA6348_15350
BRWGOP56_19910(sbnB)
ANXACH33_02520
ATHEK3F53_05635 K3F53_16430(sbnB)
SACAFFV09_03655(sbnB)
TUMCBW65_11390
TABCIG75_16790
LFBC1X05_04235
KPULGXN76_14220(sbnB)
PABSJIR001_05100(sbnB)
SACGFDZ84_26435(sbnB)
PMADBAY61_28575
AFLOHEQ12_15470(sbnB)
PPIOCE91St28_22640(ocd2)
 » show all
Reference
1  [PMID:21906287]
  Authors
Beasley FC, Cheung J, Heinrichs DE
  Title
Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus.
  Journal
BMC Microbiol 11:199 (2011)
DOI:10.1186/1471-2180-11-199
Reference
2  [PMID:24485762]
  Authors
Kobylarz MJ, Grigg JC, Takayama SJ, Rai DK, Heinrichs DE, Murphy ME
  Title
Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor.
  Journal
Chem Biol 21:379-88 (2014)
DOI:10.1016/j.chembiol.2013.12.011
  Sequence
[sae:NWMN_0061]
Other DBs
ExplorEnz - The Enzyme Database: 1.5.1.51
IUBMB Enzyme Nomenclature: 1.5.1.51
ExPASy - ENZYME nomenclature database: 1.5.1.51
BRENDA, the Enzyme Database: 1.5.1.51
LinkDB

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