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
ec00470  D-Amino acid metabolism
ec01100  Metabolic pathways
Orthology
K10793  D-proline reductase (dithiol) PrdA
K10794  D-proline reductase (dithiol) PrdB
Genes
GEBGM18_3141
GURGura_0093
DEUDBW_0111(prdB_1) DBW_1884(prdB_2)
DVEDESUT3_02860
DRTDret_0950
ADEAdeh_1149
ACPA2cp1_1279
AFWAnae109_1196
ANKAnaeK_1209
AORYAMOR_09570(prdB)
SCUSCE1572_36590 SCE1572_36595
HOHHoch_1982
DTIDesti_3193
DHRLGS26_09520
BDAFSZ17_12580
BACIB1NLA3E_03255
NMKCHR53_14760
AIAAWH56_012720 AWH56_019995
CTHUHUR95_07565 HUR95_11100 HUR95_16825
BBEVBBEV_2875
BSEBsel_0470
STEAC0679_01850(prdA) C0679_01860(prdB)
GOTAXE85_07500 AXE85_07510 AXE85_08095 AXE85_08105
GMONCTC11323_00111(prdA_1) NCTC11323_00113(prdB_1)
GEQCG018_01110(prdB) CG018_01120(prdA) CG018_01690(prdB) CG018_01700(prdA)
GSAFOC50_03415(prdB) FOC50_03425(prdA)
EFFskT53_13920(prdB)
PMARB0X71_08520
PGQFK545_19640
PLAYDNR44_005140 DNR44_016870
LSJLSJ_2016
LALWBTM29_06305 BTM29_06315
EHREHR_11635
EGVEGCR1_16890(prdB) EGCR1_16900(prdA) EGCR1_17750(prdA) EGCR1_17760(prdB)
EAVEH197_04395(prdB) EH197_04405(prdA)
ERAFJ9537_18460(prdA) J9537_18470(prdB)
MPSMPTP_0392 MPTP_0394
MPXMPD5_1504 MPD5_1506
VAOFA707_05395(prdA) FA707_05405(prdB)
VCPH9L18_10975(prdB) H9L18_10985(prdA)
VHYG7082_09795(prdA) G7082_09805(prdB)
DPMFNV33_08285
CBOCBO2461(prdB1) CBO2464(prdA1) CBO2477(prdB2) CBO2480(prdA2)
CBACLB_2328(prdB) CLB_2330(prdA) CLB_2347(prdB) CLB_2349(prdA)
CBHCLC_2313 CLC_2331(prdA)
CBYCLM_2757(prdB) CLM_2759(prdA) CLM_2774 CLM_2776(prdA)
CBLCLK_1840(prdB) CLK_1843(prdA) CLK_1858 CLK_1861(prdA) CLK_3048(prdB-2) CLK_3050
CBBCLD_2158(prdA) CLD_2160 CLD_2175(prdA) CLD_2177(prdB)
CBICLJ_B2689(prdB) CLJ_B2691(prdA_1) CLJ_B2705 CLJ_B2707(prdA_2)
CBFCLI_2520 CLI_2522(prdA) CLI_2537(prdB-1) CLI_2539 CLI_3800(prdB-2) CLI_3802
CBMCBF_2512 CBF_2530 CBF_3766(prdB-2) CBF_3768
CBJH04402_02490 H04402_02492 H04402_02506 H04402_02508
CSQCSCA_3974 CSCA_3976 CSCA_3983 CSCA_3985 CSCA_4535 CSCA_4537
CLDCLSPO_c25610(prdB2) CLSPO_c25630(prdA2) CLSPO_c25730(prdB3) CLSPO_c25750(prdA3) CLSPO_c37590(prdB1) CLSPO_c37600(prdA1)
CCKCcar_21400 Ccar_21410 Ccar_21445 Ccar_21455
CTYKCTK_C02870(prdA) CTK_C02890(prdB)
CARGRSJ17_05070
CDRKB9W14_22330 B9W14_22340 B9W14_25190 B9W14_25200 B9W14_25230 B9W14_25240
CFERD4Z93_00645(prdA) D4Z93_00655(prdB) D4Z93_07400(prdB) D4Z93_07410(prdA)
CCAAKQH81_13630(prdB) KQH81_13640(prdA)
CMAHC1I91_24425(prdB) C1I91_24435(prdA)
AMTAmet_0665 Amet_0667
AOEClos_0028 Clos_0030
GFEGferi_10125 Gferi_10135
CALEFDN13_14090(prdA) FDN13_14100(prdB)
CRASKVH43_09135(prdA) KVH43_09145(prdB)
PBIFKXZ80_01755(prdA) KXZ80_01765(prdB)
CCOMI6K69_12530(prdA) I6K69_12540(prdB)
CSCIHDCHBGLK_00540(prdB) HDCHBGLK_00542(prdA_4)
DLOK5I24_06915(prdB) K5I24_06925(prdA)
SINTK5I26_00370(prdB) K5I26_00380(prdA)
CDFCD630_32410(prdB) CD630_32440(prdA)
PDCCDIF630_03537(prdB) CDIF630_03540(prdA)
CDCCD196_3057(prdA)
CDLCDR20291_3101(prdB) CDR20291_3103(prdA)
PDFCD630DERM_32410(prdB) CD630DERM_32440(prdA)
EACEAL2_808p02680(prdA)
CSTCLOST_2232(pdrB) CLOST_2234(prdA)
PSORRSJ16_01990
PHXKGNDJEFE_00578(prdA_2) KGNDJEFE_00580(prdB_1)
TEMJW646_10395(prdA) JW646_10405(prdB) JW646_20070(prdB) JW646_20080(prdA)
TGCL0P85_17390(prdB) L0P85_17400(prdA)
TEBT8CH_2594 T8CH_2596(prdA) T8CH_2603 T8CH_2605(prdA)
STHSTH1055
MDVC5Q96_04745(prdB) C5Q96_04755(prdA)
CCHAELD05_12220(prdB) ELD05_12230(prdA)
TOCToce_1679 Toce_1681 Toce_1683
NTHNther_2712
NCDACONDI_01659(prdA)
AFTBBF96_15365 BBF96_15375
PIVNCTC13079_00345(prdA_2) NCTC13079_00347(prdB_1) NCTC13079_00352(prdA_4) NCTC13079_00354(prdB_2)
KPARJL105_02455(prdA) JL105_02465
SEDZJYG23_00365(prdA) JYG23_00375(prdB)
MEDMELS_0425 MELS_0427
MMAXLCQ47_08860(prdA) LCQ47_08870
SAPISAPIS_v1c05020(prdA) SAPIS_v1c05040(prdB)
SALXSALLE_v1c01990(prdA) SALLE_v1c02010(prdB)
SCHISCHIN_v1c02000(prdA) SCHIN_v1c02020(prdB)
PBOPACID_24380 PACID_24400
AACIASQ49_09810
BTPD805_1400 D805_1402
BSUEBS3272_00510(prdA) BS3272_00520(prdB)
RXYRxyl_2192
RRDRradSPS_1992 RradSPS_2041
RUBGBA63_14520
RMARGBA65_05300
CAUCaur_0049
CHLChy400_0055
HAUHaur_4406
CAPCLDAP_39700(prdB)
KBSEPA93_08670 EPA93_19735
CTMCabther_B0068
CVLJ8C06_14165
CHLOJ8C02_13015
 » 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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