T3HPD_PSEAE
ID T3HPD_PSEAE Reviewed; 344 AA.
AC Q9I489;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable trans-3-hydroxy-L-proline dehydratase {ECO:0000305};
DE Short=T3LHyp dehydratase;
DE Short=t3HypD;
DE EC=4.2.1.77 {ECO:0000305|PubMed:24980702};
DE AltName: Full=Trans-L-3-hydroxyproline dehydratase;
GN OrderedLocusNames=PA1255;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP LACK OF ENZYMATIC ACTIVITY AS PROLINE RACEMASE AND
RP HYDROXYPROLINE-2-EPIMERASE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=17849014; DOI=10.1371/journal.pone.0000885;
RA Goytia M., Chamond N., Cosson A., Coatnoan N., Hermant D., Berneman A.,
RA Minoprio P.;
RT "Molecular and structural discrimination of proline racemase and
RT hydroxyproline-2-epimerase from nosocomial and bacterial pathogens.";
RL PLoS ONE 2:E885-E885(2007).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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: Probably catalyzes the dehydration of trans-3-hydroxy-L-
CC proline (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.aeruginosa to grow on t3LHyp as a sole carbon
CC source (PubMed:24980702). Displays neither trans-4-hydroxy-L-proline
CC (t4LHyp) epimerase nor proline racemase activity (PubMed:17849014).
CC {ECO:0000269|PubMed:17849014, ECO:0000305|PubMed:24980702}.
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:0000305|PubMed:24980702};
CC -!- INDUCTION: Is up-regulated when the bacterium is grown on trans-4-
CC hydroxy-L-proline (t4LHyp) or trans-3-hydroxy-L-proline (t3LHyp) as
CC sole carbon source. {ECO:0000269|PubMed:24980702}.
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04644.1; -; Genomic_DNA.
DR PIR; E83488; E83488.
DR RefSeq; NP_249946.1; NC_002516.2.
DR RefSeq; WP_003114965.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I489; -.
DR SMR; Q9I489; -.
DR STRING; 287.DR97_682; -.
DR PaxDb; Q9I489; -.
DR PRIDE; Q9I489; -.
DR DNASU; 881287; -.
DR EnsemblBacteria; AAG04644; AAG04644; PA1255.
DR GeneID; 881287; -.
DR KEGG; pae:PA1255; -.
DR PATRIC; fig|208964.12.peg.1303; -.
DR PseudoCAP; PA1255; -.
DR HOGENOM; CLU_036729_2_0_6; -.
DR InParanoid; Q9I489; -.
DR OMA; IMESEEY; -.
DR PhylomeDB; Q9I489; -.
DR BioCyc; PAER208964:G1FZ6-1280-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0047580; F:4-hydroxyproline epimerase activity; IMP:PseudoCAP.
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..344
FT /note="Probable trans-3-hydroxy-L-proline dehydratase"
FT /id="PRO_0000354047"
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 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 257..258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
SQ SEQUENCE 344 AA; 37344 MW; BFBFB4BDFB6342F5 CRC64;
MRSQRIVHIV SCHAEGEVGD VIVGGVAAPP GATLWEQSRW IARDQDLRNF VLNEPRGGVF
RHANLLVPAK DPRAQMGWII MEPADTPPMS GSNSLCVATV LLDSGILPMR EPLTRLLLEA
PGGLIEARAE CRDGKAERVE IRNVPSFADR LDAWIEVEGL GSLQVDTAYG GDSFVIADAR
RLGFALRADE AAELVATGLK ITHAANEQLG FRHPTNPDWD HLSFCQLAAP PERRDGVLGA
NNAVVIRPGK IDRSPCGTGC SARMAVLQAK GQLRVGERFV GRSIIGSEFH CHIESLTELG
GRPAILPCLS GRAWITGIHQ YLLDPDDPWP QGYRLSDTWP GGHC
