T3HPD_PARDP
ID T3HPD_PARDP Reviewed; 342 AA.
AC A1B195;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Trans-3-hydroxy-L-proline dehydratase {ECO:0000303|PubMed:24980702};
DE Short=T3LHyp dehydratase;
DE Short=t3HypD {ECO:0000303|PubMed:24980702};
DE EC=4.2.1.77 {ECO:0000269|PubMed:24980702};
DE AltName: Full=Trans-L-3-hydroxyproline dehydratase;
GN OrderedLocusNames=Pden_1184 {ECO:0000312|EMBL:ABL69289.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Pd 1222;
RX PubMed=24980702; DOI=10.7554/elife.03275;
RA Zhao S., Sakai A., Zhang X., Vetting M.W., Kumar R., Hillerich B.,
RA San Francisco B., Solbiati J., Steves A., Brown S., Akiva E., Barber A.,
RA Seidel R.D., Babbitt P.C., Almo S.C., Gerlt J.A., Jacobson M.P.;
RT "Prediction and characterization of enzymatic activities guided by sequence
RT similarity and genome neighborhood networks.";
RL Elife 3:E03275-E03275(2014).
CC -!- FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline
CC (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely
CC involved in a degradation pathway that converts t3LHyp to L-proline,
CC which would allow P.denitrificans to grow on t3LHyp as a sole carbon
CC source. Displays neither proline racemase activity nor 4-hydroxyproline
CC 2-epimerase activity. {ECO:0000269|PubMed:24980702, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=trans-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O;
CC Xref=Rhea:RHEA:10320, ChEBI:CHEBI:15377, ChEBI:CHEBI:39785,
CC ChEBI:CHEBI:57938; EC=4.2.1.77;
CC Evidence={ECO:0000269|PubMed:24980702};
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; CP000489; ABL69289.1; -; Genomic_DNA.
DR RefSeq; WP_011747509.1; NC_008686.1.
DR AlphaFoldDB; A1B195; -.
DR SMR; A1B195; -.
DR STRING; 318586.Pden_1184; -.
DR PRIDE; A1B195; -.
DR EnsemblBacteria; ABL69289; ABL69289; Pden_1184.
DR KEGG; pde:Pden_1184; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_2_0_5; -.
DR OMA; ANDWSHI; -.
DR Proteomes; UP000000361; Chromosome 1.
DR GO; GO:0050346; F:trans-L-3-hydroxyproline dehydratase activity; IEA:UniProtKB-EC.
DR InterPro; IPR008794; Pro_racemase_fam.
DR PANTHER; PTHR33442; PTHR33442; 1.
DR Pfam; PF05544; Pro_racemase; 1.
DR PIRSF; PIRSF029792; Pro_racemase; 1.
DR SFLD; SFLDS00028; Proline_Racemase; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..342
FT /note="Trans-3-hydroxy-L-proline dehydratase"
FT /id="PRO_0000432270"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
SQ SEQUENCE 342 AA; 37450 MW; 0BB9E98622B9AB21 CRC64;
MRTSRVVHVV SCHAEGEVGD VIVGGVAPPP GETVWDQSRW IARDETLRNF VLNEPRGGVF
RHVNLLVPPK DPRAQMGWII MEPADTPPMS GSNAICVATV LLDTGIIPMQ EPITRMVLEP
PGGLIEVEAE CRGGKAERIR VRNVPSFADR LDARIEVEGL GTITVDTAYG GDSFVLVDAA
SVGMRIAPDQ ARDLAEMGVR ITRAANEQLG FRHPANDWSH ISFCQFTDPL SERDGVLYGR
NAVAIRPGKI DRSPTGTGCS ARMAVLHARG RMKPGDRFVG RSIIDTEFHC SIADEVELNG
KRAIRPIISG RAWVIGTKQL MVDPDDPFQN GYRLSDTWPM DL