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Entry
EC 1.21.4.4                 Enzyme                                 

Name
betaine reductase;
acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (N,N,N-trimethylglycine-forming)
Class
Oxidoreductases;
Catalysing the reaction X-H + Y-H = X-Y;
With a disulfide as acceptor
BRITE hierarchy
Sysname
acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (betaine-forming)
Reaction(IUBMB)
acetyl phosphate + trimethylamine + thioredoxin disulfide + H2O = betaine + phosphate + thioredoxin [RN:R07228]
Reaction(KEGG)
Substrate
acetyl phosphate [CPD:C00227];
trimethylamine [CPD:C00565];
thioredoxin disulfide [CPD:C00343];
H2O [CPD:C00001]
Product
betaine [CPD:C00719];
phosphate [CPD:C00009];
thioredoxin [CPD:C00342]
Comment
The reaction is observed only in the direction of betaine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for betaine binding and trimethylamine release. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.2 (glycine reductase) and EC 1.21.4.3 (sarcosine reductase).
History
EC 1.21.4.4 created 2003, modified 2010
Orthology
K10670  glycine/sarcosine/betaine reductase complex component A
K21576  glycine/sarcosine/betaine reductase complex component C subunit alpha
K21577  glycine/sarcosine/betaine reductase complex component C subunit beta
K21578  betaine reductase complex component B subunit alpha
K21579  betaine reductase complex component B subunit beta
Genes
EFE: EFER_3016 EFER_3017 EFER_3018 EFER_3019
PPR: PBPRB1546(PLSX2) PBPRB1547(FABH4) PBPRB1548 PBPRB1549
PGB: H744_1c1273 H744_1c1274 H744_1c1275 H744_1c1276
DDS: Ddes_0115 Ddes_0116 Ddes_0118
DFI: AXF13_12700 AXF13_12705 AXF13_12715 AXF13_12720
DPG: DESPIGER_2436 DESPIGER_2442 DESPIGER_2443 DESPIGER_2445
DEF: CNY67_00630 CNY67_00635 CNY67_00645
DEO: CAY53_05570
SAT: SYN_00806 SYN_03718
DTI: Desti_4380 Desti_4381 Desti_4382
CBO: CBO1264(grdD)
CBA: CLB_1290(grdA) CLB_1291(grdC) CLB_1292(grdD)
CBH: CLC_1301(grdC) CLC_1302(grdD)
CBY: CLM_1420(grdA) CLM_1421(grdA) CLM_1422(grdC) CLM_1423(grdD)
CBL: CLK_0701(grdA) CLK_0702 CLK_0703(grdC) CLK_0704(grdD)
CBB: CLD_3303(grdD) CLD_3304(grdC) CLD_3305(grdA) CLD_3306
CBI: CLJ_B1306(grdC) CLJ_B1307(grdD)
CBF: CLI_1346(grdA) CLI_1347(grdC) CLI_1348(grdD)
CBM: CBF_1319(grdA) CBF_1320(grdA) CBF_1321(grdC) CBF_1322(grdD)
CLD: CLSPO_c12690(grdA) CLSPO_c12700(grdC) CLSPO_c12710(grdD) CLSPO_c14800(grdI) CLSPO_c14810(grdH)
CACE: CACET_c07270(grdA1) CACET_c07280(grdC1) CACET_c07290(grdD1) CACET_c07300(grdI) CACET_c07310(grdH) CACET_c12290(grdA2) CACET_c12310(grdC2) CACET_c12320(grdD2)
CDF: CD630_23480(grdD) CD630_23490(grdC) CD630_23520(grdA)
PDC: CDIF630_02587(grdD) CDIF630_02588(grdC) CDIF630_02592(grdA)
CDC: CD196_2191(grdD) CD196_2192(grdC)
CDL: CDR20291_2237(grdD) CDR20291_2238(grdC) CDR20291_2240(grdA)
EAC: EAL2_808p07350(grdA4) EAL2_c02900(grdI) EAL2_c02910(grdH) EAL2_c02950(grdC2) EAL2_c02960(grdD2) EAL2_c08740(grdA2) EAL2_c16950(grdD) EAL2_c16960(grdC) EAL2_c16970(grdA1) EAL2_c17010(grdA3)
CST: CLOST_1056(grdI) CLOST_1057(grdH) CLOST_1112(grdA) CLOST_1115(grdC) CLOST_1116(grdD)
TTE: TTE1874(PlsX2) TTE1875(FabH4)
CHY: CHY_2392(grdA) CHY_2394(grdC) CHY_2395(grdD)
TDE: TDE0239(grdD) TDE0240(grdC) TDE0745(grdA)
BPO: BP951000_1855(grdA) BP951000_1857(grdC) BP951000_1858(grdC)
SBR: SY1_16370
BARC: AOA65_0941 AOA65_0944(grdA)
 » show all
Taxonomy
Reference
1  [PMID:10091582]
  Authors
Wagner M, Sonntag D, Grimm R, Pich A, Eckerskorn C, Sohling B, Andreesen JR.
  Title
Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis.
  Journal
Eur J Biochem 260:38-49 (1999)
DOI:10.1046/j.1432-1327.1999.00107.x
  Sequence
Reference
2  [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
Other DBs
ExplorEnz - The Enzyme Database: 1.21.4.4
IUBMB Enzyme Nomenclature: 1.21.4.4
ExPASy - ENZYME nomenclature database: 1.21.4.4
BRENDA, the Enzyme Database: 1.21.4.4
CAS: 125752-87-6

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