KEGG   ENZYME: 1.21.4.1
Entry
EC 1.21.4.1                 Enzyme                                 

Name
D-proline reductase;
prdAB (gene names);
D-proline reductase (dithiol)
Class
Oxidoreductases;
Catalysing the reaction X-H + Y-H = X-Y;
With a disulfide as acceptor
Sysname
5-aminopentanoate:[PrdC protein] oxidoreductase (cyclizing)
Reaction(IUBMB)
5-aminopentanoate + a [PrdC protein with a selenide-sulfide bridge] = D-proline + a [PrdC protein with thiol/selenol residues]
Reaction(KEGG)
(other) R02825
Substrate
5-aminopentanoate [CPD:C00431];
[PrdC protein with a selenide-sulfide bridge]
Product
D-proline [CPD:C00763];
[PrdC protein with thiol/selenol residues]
Comment
A pyruvoyl- and L-selenocysteine-containing enzyme found in a number of Clostridial species. The pyruvoyl group, located on the PrdA subunit, binds the substrate, while the selenocysteine residue, located on the PrdB subunit, attacks the alpha-C-atom of D-proline, leading to a reductive cleavage of the C-N-bond of the pyrrolidine ring and formation of a selenoether. The selenoether is cleaved by a cysteine residue of PrdB, resulting in a mixed selenide-sulfide bridge, which is restored to its reduced state by another selenocysteine protein, PrdC. 5-aminopentanoate is released from PrdA by hydrolysis, regenerating the pyruvoyl moiety. The resulting mixed selenide-sulfide bridge in PrdC is reduced by NADH.
History
EC 1.21.4.1 created 1972 as EC 1.4.4.1, modified 1982 (EC 1.4.1.6 created 1961, incorporated 1982), transferred 2003 to EC 1.21.4.1, modified 2018
Pathway
ec00330  Arginine and proline metabolism
ec01100  Metabolic pathways
Orthology
K10793  D-proline reductase (dithiol) PrdA
K10794  D-proline reductase (dithiol) PrdB
Genes
PDQ: CL55_00001970
BPC: BPTD_0387
BPER: BN118_3228
BPET: B1917_0394
BPEU: Q425_34440
BPAR: BN117_4434
BPA: BPP4301
BBH: BN112_3538
BBR: BB4888
BBM: BN115_4558
AOA: dqs_2522
BPRC: D521_0194
GUR: Gura_0093
GEB: GM18_3141
DEU: DBW_0111(prdB_1) DBW_1884(prdB_2)
DRT: Dret_0950
ADE: Adeh_1149
HOH: Hoch_1982
RPC: RPC_3322
RPD: RPD_3052
RBM: TEF_14805
BBEV: BBEV_2875
STEA: C0679_01850(prdA) C0679_01860(prdB)
BSE: Bsel_0470
GMO: NCTC11323_00111(prdA_1) NCTC11323_00113(prdB_1)
GEQ: CG018_01110(prdB) CG018_01120(prdA) CG018_01690(prdB) CG018_01700(prdA)
GSA: FOC50_03415(prdB) FOC50_03425(prdA)
LSJ: LSJ_2016
EHR: EHR_11635
EGV: EGCR1_16890(prdB) EGCR1_16900(prdA) EGCR1_17750(prdA) EGCR1_17760(prdB)
EAV: EH197_04395(prdB) EH197_04405(prdA)
VAO: FA707_05395(prdA) FA707_05405(prdB)
CBO: CBO2480(prdA2)
CBA: CLB_2328(prdB) CLB_2330(prdA) CLB_2347(prdB) CLB_2349(prdA)
CBH: CLC_2313 CLC_2331(prdA)
CBY: CLM_2757(prdB) CLM_2759(prdA) CLM_2774 CLM_2776(prdA)
CBL: CLK_1840(prdB) CLK_1843(prdA) CLK_1858 CLK_1861(prdA) CLK_3048(prdB-2) CLK_3050
CBB: CLD_2158(prdA) CLD_2160 CLD_2175(prdA) CLD_2177(prdB)
CBI: CLJ_B2689(prdB) CLJ_B2691(prdA_1) CLJ_B2705 CLJ_B2707(prdA_2)
CBF: CLI_2520 CLI_2522(prdA) CLI_2537(prdB-1) CLI_2539 CLI_3800(prdB-2) CLI_3802
CLD: CLSPO_c25610(prdB2) CLSPO_c25630(prdA2) CLSPO_c25730(prdB3) CLSPO_c25750(prdA3) CLSPO_c37590(prdB1) CLSPO_c37600(prdA1)
CTYK: CTK_C02870(prdA) CTK_C02890(prdB)
AMT: Amet_0665
CALE: FDN13_14090(prdA) FDN13_14100(prdB)
CSCI: HDCHBGLK_00540(prdB) HDCHBGLK_00542(prdA_4)
CDF: CD630_32410(prdB) CD630_32440(prdA)
PDC: CDIF630_03537(prdB) CDIF630_03540(prdA)
CDC: CD196_3057(prdA)
CDL: CDR20291_3101(prdB) CDR20291_3103(prdA)
EAC: EAL2_808p02680(prdA)
CST: CLOST_2232(pdrB) CLOST_2234(prdA)
PHX: KGNDJEFE_00578(prdA_2) KGNDJEFE_00580(prdB_1)
STH: STH1055
MDV: C5Q96_04745(prdB) C5Q96_04755(prdA)
CCHA: ELD05_12220(prdB) ELD05_12230(prdA)
PIV: NCTC13079_00345(prdA_2) NCTC13079_00347(prdB_1) NCTC13079_00352(prdA_4) NCTC13079_00354(prdB_2)
SAPI: SAPIS_v1c05020(prdA) SAPIS_v1c05040(prdB)
SALX: SALLE_v1c01990(prdA) SALLE_v1c02010(prdB)
RXY: Rxyl_2192
AYM: YM304_02800(prdB)
HAU: Haur_4406
CAP: CLDAP_39700(prdB)
 » show all
Reference
1  [PMID:13475375]
  Authors
STADTMAN TC, ELLIOTT P.
  Title
Studies on the enzymic reduction of amino acids. II. Purification and properties of D-proline reductase and a proline racemase from Clostridium sticklandii.
  Journal
J Biol Chem 228:983-97 (1957)
Reference
2  [PMID:5778643]
  Authors
Hodgins DS, Abeles RH.
  Title
Studies of the mechanism of action of D-proline reductase: the presence on covalently bound pyruvate and its role in the catalytic process.
  Journal
Arch Biochem Biophys 130:274-85 (1969)
DOI:10.1016/0003-9861(69)90034-4
Reference
3  [PMID:10085076]
  Authors
Kabisch UC, Grantzdorffer A, Schierhorn A, Rucknagel KP, Andreesen JR, Pich A.
  Title
Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein.
  Journal
J Biol Chem 274:8445-54 (1999)
DOI:10.1074/jbc.274.13.8445
  Sequence
Reference
4  [PMID:11422384]
  Authors
Bednarski B, Andreesen JR, Pich A.
  Title
In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue.
  Journal
Eur J Biochem 268:3538-44 (2001)
DOI:10.1046/j.1432-1327.2001.02257.x
Reference
5  [PMID:20937090]
  Authors
Fonknechten N, Chaussonnerie S, Tricot S, Lajus A, Andreesen JR, Perchat N, Pelletier E, Gouyvenoux M, Barbe V, Salanoubat M, Le Paslier D, Weissenbach J, Cohen GN, Kreimeyer A
  Title
Clostridium sticklandii, a specialist in amino acid degradation:revisiting its metabolism through its genome sequence.
  Journal
BMC Genomics 11:555 (2010)
DOI:10.1186/1471-2164-11-555
Other DBs
ExplorEnz - The Enzyme Database: 1.21.4.1
IUBMB Enzyme Nomenclature: 1.21.4.1
ExPASy - ENZYME nomenclature database: 1.21.4.1
BRENDA, the Enzyme Database: 1.21.4.1
CAS: 37255-43-9

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