KEGG   ENZYME: 2.6.1.81Help
Entry
EC 2.6.1.81                 Enzyme                                 

Name
succinylornithine transaminase;
succinylornithine aminotransferase;
N2-succinylornithine 5-aminotransferase;
AstC;
SOAT;
2-N-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase
Class
Transferases;
Transferring nitrogenous groups;
Transaminases
BRITE hierarchy
Sysname
N2-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase
Reaction(IUBMB)
N2-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate [RN:R04217]
Reaction(KEGG)
Substrate
N2-succinyl-L-ornithine [CPD:C03415];
2-oxoglutarate [CPD:C00026]
Product
N-succinyl-L-glutamate 5-semialdehyde [CPD:C05932];
L-glutamate [CPD:C00025]
Comment
A pyridoxal-phosphate protein. Also acts on N2-acetyl-L-ornithine and L-ornithine, but more slowly [3]. In Pseudomonas aeruginosa, the arginine-inducible succinylornithine transaminase, acetylornithine transaminase (EC 2.6.1.11) and ornithine aminotransferase (EC 2.6.1.13) activities are catalysed by the same enzyme, but this is not the case in all species [5]. This is the third 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 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase) [3,6].
History
EC 2.6.1.81 created 2006
Pathway
Arginine and proline metabolism
Orthology
K00840  
succinylornithine aminotransferase
Genes
ECO: 
b1748(astC)
ECJ: 
Y75_p1723(astC)
ECD: 
EBW: 
BWG_1561(astC)
ECOK: 
ECE: 
Z2780(argD)
ECS: 
ECs2454(argD)
ECF: 
ETW: 
ECSP_2316(astC)
ELX: 
EOJ: 
EOI: 
EOH: 
ECG: 
EOK: 
ELR: 
ECC: 
c2148(argD)
ECP: 
ECI: 
ECV: 
ECX: 
ECW: 
ECM: 
ECY: 
ECR: 
ECQ: 
ECK: 
ECT: 
EOC: 
CE10_2027(astC)
EUM: 
ECZ: 
ELO: 
ELN: 
ELH: 
ESE: 
ESO: 
ESM: 
ESL: 
ECL: 
EBR: 
ECB_01717(astC)
EBD: 
EKO: 
EKF: 
EAB: 
EDH: 
EDJ: 
EIH: 
ENA: 
ELU: 
EUN: 
ELW: 
ECW_m1917(astC)
ELL: 
WFL_09400(astC)
ELC: 
i14_1967(argD)
ELD: 
i02_1967(argD)
ELP: 
EBL: 
ECD_01717(astC)
EBE: 
B21_01705(astC)
ELF: 
LF82_0182(astC)
ECOA: 
ECOL: 
ECOI: 
ECOJ: 
EFE: 
EFER_1317(astC)
STY: 
STY1811(astC)
STT: 
t1182(argD)
SEX: 
SENT: 
STM: 
STM1303(argD)
SEO: 
STM14_1582(argD_1)
SEV: 
SEY: 
SEM: 
SEJ: 
SEB: 
SEF: 
SETU: 
SETC: 
SEEN: 
SENR: 
SEND: 
SPT: 
SPA1541(astC)
SEK: 
SPQ: 
SEI: 
SPC_2428(argD)
SEC: 
SC1326(argD)
SEH: 
SHB: 
SENH: 
SEEH: 
SEE: 
SENN: 
SEW: 
SEA: 
SENS: 
SED: 
SEG: 
SG1813(astC)
SEL: 
SPUL_1118(astC)
SEGA: 
SET: 
SEN1740(astC)
SENJ: 
SEEC: 
SEEB: 
SEEP: 
SENB: 
BN855_13380(SBOV12971)
SENE: 
SES: 
SBG: 
SBG_1156(astC)
SBZ: 
YPE: 
YPO1962(argD)
YPK: 
y2349(argD)
YPA: 
YPM: 
YP_1707(argD)
YPP: 
YPG: 
YPD: 
YPD4_1727(argD)
YPX: 
YPD8_1821(argD)
YPS: 
YPTB1959(argD)
YPI: 
YPY: 
YPB: 
YEN: 
YE2469(argM)
YEP: 
YEY: 
SSN: 
SSON_1409(cstC)
SSJ: 
SBO: 
SBO_1342(cstC)
SBC: 
ETA: 
ETA_18590(argM)
EPY: 
EpC_19470(argM)
EPR: 
EBI: 
EbC_18580(astC)
ERJ: 
PLU: 
plu3110(argD)
PAY: 
PAU_01497(argM)
ENT: 
ENC: 
ENO: 
ESC: 
EEC: 
ENL: 
EAS: 
EAE: 
EAR: 
ENR: 
ESA: 
CSK: 
ES15_2307(astC)
CSZ: 
CSI: 
CTU: 
CTU_18160(astC)
KPN: 
KPU: 
KPM: 
KPP: 
KPE: 
KPO: 
KPR: 
KPJ: 
KPI: 
KVA: 
KOX: 
KOE: 
CKO: 
CRO: 
ROD_13091(astC)
SPE: 
SRR: 
SRL: 
SRY: 
SRS: 
SRA: 
SMAF: 
SMW: 
SLQ: 
SERR: 
SFO: 
DDA: 
XBO: 
XBJ1_2942(argM)
PAM: 
PANA_1674(argM)
PLF: 
PAJ: 
PAJ_1024(argM)
PAQ: 
PVA: 
Pvag_1114(astC)
PAO: 
RAH: 
RAQ: 
RAA: 
ROR: 
EBF: 
VFU: 
ACI: 
ACIAD1284(argD)
ACD: 
ACB: 
ABM: 
ABSDF0355(astC)
ABY: 
ABAYE0352(astC)
ABC: 
ABN: 
ABB: 
ABX: 
ABZ: 
ABR: 
ABD: 
ABH: 
ABAD: 
ABD1_05420(astC) ABD1_11040(astC) ABD1_30200(astC)
ABJ: 
ABAB: 
ABAJ: 
ABAZ: 
ACC: 
PPK: 
PRB: 
 » show all
Taxonomy
Reference
1  [PMID:2865249]
  Authors
Vander Wauven C, Stalon V.
  Title
Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia.
  Journal
J. Bacteriol. 164 (1985) 882-6.
  Organism
Pseudomonas cepacia
Reference
2  [PMID:9696779]
  Authors
Schneider BL, Kiupakis AK, Reitzer LJ.
  Title
Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.
  Journal
J. Bacteriol. 180 (1998) 4278-86.
  Organism
Escherichia coli [GN:eco]
  Sequence
[eco:b1748]
Reference
3  [PMID:3534538]
  Authors
Cunin R, Glansdorff N, Pierard A, Stalon V.
  Title
Biosynthesis and metabolism of arginine in bacteria.
  Journal
Microbiol. Rev. 50 (1986) 314-52.
  Organism
Pseudomonas spp.
Reference
4  [PMID:9393691]
  Authors
Itoh Y.
  Title
Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.
  Journal
J. Bacteriol. 179 (1997) 7280-90.
  Organism
Pseudomonas aeruginosa [GN:pae]
  Sequence
[up:O30508]
Reference
5  [PMID:3129535]
  Authors
Stalon V, Vander Wauven C, Momin P, Legrain C.
  Title
Catabolism of arginine, citrulline and ornithine by Pseudomonas and related bacteria.
  Journal
J. Gen. Microbiol. 133 (1987) 2487-95.
  Organism
Pseudomonas cepacia, Pseudomonas putida, Pseudomonas indigofera
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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