| Entry |
|
| Name |
succinylglutamate-semialdehyde dehydrogenase;
succinylglutamic semialdehyde dehydrogenase;
N-succinylglutamate 5-semialdehyde dehydrogenase;
SGSD;
AruD;
AstD |
| Class |
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
 |
| Sysname |
N-succinyl-L-glutamate 5-semialdehyde:NAD+ oxidoreductase |
| Reaction(IUBMB) |
N-succinyl-L-glutamate 5-semialdehyde + NAD+ + H2O =
N-succinyl-L-glutamate + NADH + 2 H+ [RN:R05049] |
| Reaction(KEGG) |
R05049
 |
| Substrate |
N-succinyl-L-glutamate 5-semialdehyde [CPD:C05932];
NAD+ [CPD:C00003];
H2O [CPD:C00001] |
| Product |
N-succinyl-L-glutamate [CPD:C05931];
NADH [CPD:C00004];
H+ [CPD:C00080] |
| Comment |
This is the fourth enzyme in the arginine succinyltransferase (AST)
pathway for the catabolism of arginine [1]. This pathway converts
the carbon skeleton of arginine into glutamate, with the concomitant
production of ammonia and conversion of succinyl-CoA into succinate
and CoA. The five enzymes involved in this pathway are EC 2.3.1.109
(arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine
dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC
1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC
3.5.1.96 (succinylglutamate desuccinylase) [3,6]. |
| Pathway |
PATH: ec00330 Arginine and proline metabolism |
| Orthology |
KO: K06447 succinylglutamic semialdehyde dehydrogenase |
| Genes |
ECO: b1746(astD)
ECJ: JW5282(astD)
ECD: ECDH10B_1884(astD)
EBW: BWG_1559(astD)
ECE: Z2778(astD)
ECS: ECs2452(astD)
ECF: ECH74115_2464(astD)
ETW: ECSP_2314(astD)
ECG: E2348C_1874(astD)
ECC: c2146(astD)
ECI: UTI89_C1941(astD)
ECP: ECP_1692(astD)
ECV: APECO1_815(thrL)
ECW: EcE24377A_1968(astD)
ECX: EcHS_A1829(astD)
ECM: EcSMS35_1445(astD)
ECY: ECSE_1916(astD)
ECL: EcolC_1886(astD)
ECK: EC55989_1914(astD)
ECQ: ECED1_1948(astD)
ECR: ECIAI1_1807(astD)
ECT: ECIAI39_1308(astD)
ECZ: ECS88_1798(astD)
EUM: ECUMN_2035(astD)
ELF: LF82_0183(astD)
EBL: B21_01703(astD)
EBD: ECBD_1899
EBR: ECB_01715(astD)
EOH: ECO103_1939(astD)
EOI: ECO111_2257(astD)
EOJ: ECO26_2521(astD)
EFE: EFER_1319(astD)
STY: STY1809(astD)
STT: t1184(astD)
SPT: SPA1539(astD)
SEK: SSPA1430(astD)
SPQ: SPAB_02038(astD)
SEI: SPC_2426(astD)
SEH: SeHA_C1432(astD)
SEE: SNSL254_A1417(astD)
SEW: SeSA_A1400(astD)
SEA: SeAg_B1868(astD)
SED: SeD_A2041(astD)
SEG: SG1811(astD)
SET: SEN1738(astD)
SES: SARI_01674(astD)
STM: STM1305(astD)
YPE: YPO1964(astD)
YPK: y2347(astD)
YPM: YP_1709(astD)
YPA: YPA_1346(astD)
YPG: YpAngola_A2518(astD)
YPP: YPDSF_1159(astD)
YPS: YPTB1961(astD)
YPI: YpsIP31758_2119(astD)
YPY: YPK_2227(astD)
YPB: YPTS_2013(astD)
YEN: YE2467(astD)
SFL: SF1480
SFX: S1597(astD)
SFV: SFV_1474(astD)
SBO: SBO_1344(astD)
SBC: SbBS512_E1993(astD)
SDY: SDY_1531
ETA: ETA_18570(astD)
PLU: plu3108(astD)
PAY: PAU_01499(astD)
ENT: Ent638_1698
ESA: ESA_02155
CTU: Ctu_18180(astD)
KPN: KPN_01223(astD)
KPE: KPK_2966 KPK_3220(astD)
KPU: KP1_2253(astD) KP1_2501(astD)
CKO: CKO_01772
SPE: Spro_2842(astD)
DDA: Dd703_0486
VCH: VC2616(astD)
VCO: VC0395_A2193(astD)
VCM: VCM66_2536(aruD)
VCJ: VCD_001747
VVU: VV1_1315(astD)
VVY: VV3052(astD)
VPA: VP2795(astD)
VHA: VIBHAR_00077(astD)
VSP: VS_2859(astD)
VEX: VEA_002277
VFI: VF_2282(astD)
VFM: VFMJ11_2394(astD)
VSA: VSAL_I2735(astD)
PPR: PBPRA0291(astD)
PAE: PA0898(astD)
PAU: PA14_52670(astD)
PAP: PSPA7_4617(astD)
PAG: PLES_44181(astD)
PPU: PP_4478(astD)
PPF: Pput_1437(astD)
PPG: PputGB1_3983(astD)
PPW: PputW619_3767(astD)
PST: PSPTO_1835(astD)
PSB: Psyr_3562(astD)
PSP: PSPPH_3518(astD)
PFL: PFL_4512(astD)
PFO: Pfl01_4282(astD)
PFS: PFLU4754
PEN: PSEEN3879(astD)
PMY: Pmen_2908(astD)
ACI: ACIAD1287(astD)
ACB: A1S_3130
ABM: ABSDF0357(astD)
ABY: ABAYE0354(astD)
ABC: ACICU_03332
ABN: AB57_3585(astD)
ABB: ABBFA_000379(astD)
SON: SO_0619(astD)
SDN: Sden_1056(astD) Sden_3191(astD)
SAZ: Sama_1626(astD) Sama_3009(astD)
SBL: Sbal_0573(astD)
SBM: Shew185_3752(astD)
SBN: Sbal195_3878(astD)
SBP: Sbal223_3695(astD)
SLO: Shew_0580(astD)
SPC: Sputcn32_0647(astD)
SSE: Ssed_0811(astD)
SPL: Spea_3514(astD)
SHE: Shewmr4_0613(astD)
SHN: Shewana3_0612(astD)
SHL: Shal_3608(astD)
SWD: Swoo_0657(astD)
SWP: swp_0749(astD)
ILO: IL2316
CPS: CPS_0634(astD)
PHA: PSHAa0196(astD) PSHAb0426(astD)
PAT: Patl_0649
MAQ: Maqu_3316
AMC: MADE_00496
TTU: TERTU_2360(astD)
LPN: lpg1707(astD)
LPF: lpl1666(astD)
LPP: lpp1672(astD)
LPC: LPC_1136(astD)
HCH: HCH_01950(aruD)
CSA: Csal_2805
MMW: Mmwyl1_3670
AHA: AHA_3178(astD)
ASA: ASA_1136(astD)
KKO: Kkor_0786
CVI: CV_1499(astD)
BMA: BMA0594(astD)
BMV: BMASAVP1_A2422(astD)
BML: BMA10229_A2869(astD)
BMN: BMA10247_1733
BPS: BPSL2387(astD)
BPM: BURPS1710b_2843(astD)
BPL: BURPS1106A_2782(astD)
BPD: BURPS668_2724(astD)
BPR: GBP346_A2904(astD)
BTE: BTH_I1778(astD)
BVI: Bcep1808_1102(astD)
BUR: Bcep18194_A4294(astD)
BCM: Bcenmc03_1160(astD)
BCJ: BCAL1062(astD)
BAM: Bamb_1064(astD)
BAC: BamMC406_1064(astD)
BMU: Bmul_2121(astD)
BMJ: BMULJ_01123(astD)
BXE: Bxe_A2920(astD)
BPH: Bphy_1784(astD)
BPY: Bphyt_1561(astD)
BGL: bglu_1g10130
BBA: Bd0131(astD)
SCL: sce0676(astD)
CCR: CC_0582 CC_1607
CCS: CCNA_00618 CCNA_01679
CAK: Caul_2203
HNE: HNE_1995(astD)
HBA: Hbal_1559
ZMO: ZMO1272
ZMN: Za10_0068
NAR: Saro_0939(astD)
SAL: Sala_0773(astD)
SWI: Swit_0529
 |
| Structures |
PDB: 3JU8 |
Reference Authors Title
Journal Organism
|
1 [PMID:3144259]
Vander Wauven C, Jann A, Haas D, Leisinger T, Stalon V.
N2-succinylornithine in ornithine catabolism of Pseudomonas
aeruginosa.
Arch. Microbiol. 150 (1988) 400-4.
Pseudomonas aeruginosa [GN:pae] |
Reference Authors Title
Journal Organism
|
2 [PMID:2865249]
Vander Wauven C, Stalon V.
Occurrence of succinyl derivatives in the catabolism of arginine in
Pseudomonas cepacia.
J. Bacteriol. 164 (1985) 882-6.
Pseudomonas cepacia |
Reference Authors Title
Journal Organism
|
3 [PMID:7523119]
Tricot C, Vander Wauven C, Wattiez R, Falmagne P, Stalon V.
Purification and properties of a succinyltransferase from
Pseudomonas aeruginosa specific for both arginine and ornithine.
Eur. J. Biochem. 224 (1994) 853-61.
Pseudomonas aeruginosa [GN:pae] |
Reference Authors Title
Journal Organism
|
4 [PMID:9393691]
Itoh Y.
Cloning and characterization of the aru genes encoding enzymes of
the catabolic arginine succinyltransferase pathway in Pseudomonas
aeruginosa.
J. Bacteriol. 179 (1997) 7280-90.
Pseudomonas aeruginosa [GN:pae] |
Reference Authors Title
Journal Organism
|
5 [PMID:9696779]
Schneider BL, Kiupakis AK, Reitzer LJ.
Arginine catabolism and the arginine succinyltransferase pathway in
Escherichia coli.
J. Bacteriol. 180 (1998) 4278-86.
Escherichia coli [GN:eco] |
Reference Authors Title Journal Organism
|
6 [PMID:3534538]
Cunin R, Glansdorff N, Pierard A, Stalon V.
Biosynthesis and metabolism of arginine in bacteria.
Microbiol. Rev. 50 (1986) 314-52.
Pseudomonas cepacia |
Reference Authors Title Journal
|
7
Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V.
Erratum report: Biosynthesis and metabolism of arginine in bacteria.
Microbiol. Rev. 51 (1987) 178. |
| Other DBs |
ExplorEnz - The Enzyme Database: 1.2.1.71
IUBMB Enzyme Nomenclature: 1.2.1.71
ExPASy - ENZYME nomenclature database: 1.2.1.71
BRENDA, the Enzyme Database: 1.2.1.71 |