ID   T3HPD_ROSAI             Reviewed;         341 AA.
AC   A0NXQ9;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
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   ORFNames=SIAM614_28502 {ECO:0000312|EMBL:EAV42586.1};
OS   Roseibium aggregatum (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC
OS   16684 / NCIMB 2208 / IAM 12614 / B1) (Stappia aggregata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Roseibium.
OX   NCBI_TaxID=384765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM
RC   12614 / B1;
RA   King G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC   STRAIN=ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM
RC   12614 / B1;
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). May be involved
CC       in a degradation pathway of t3LHyp, which would allow L.aggregata to
CC       grow on t3LHyp as a sole carbon source. Displays neither proline
CC       racemase activity nor 4-hydroxyproline 2-epimerase activity.
CC       {ECO:0000269|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:0000269|PubMed:24980702};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.8 mM for trans-3-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 15 sec(-1) for t3LHyp dehydration.
CC         {ECO:0000269|PubMed:24980702};
CC   -!- INDUCTION: Is up-regulated when the bacterium is grown on t4LHyp or
CC       t3LHyp as sole carbon source. {ECO:0000269|PubMed:24980702}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; AAUW01000014; EAV42586.1; -; Genomic_DNA.
DR   RefSeq; WP_006937106.1; NZ_AAUW01000014.1.
DR   AlphaFoldDB; A0NXQ9; -.
DR   SMR; A0NXQ9; -.
DR   eggNOG; COG3938; Bacteria.
DR   OrthoDB; 559014at2; -.
DR   SABIO-RK; A0NXQ9; -.
DR   Proteomes; UP000004848; Unassembled WGS sequence.
DR   GO; GO:0050346; F:trans-L-3-hydroxyproline dehydratase activity; IDA:CACAO.
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.
FT   CHAIN           1..341
FT                   /note="Trans-3-hydroxy-L-proline dehydratase"
FT                   /id="PRO_0000432271"
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   341 AA;  36291 MW;  168E2D45B5E3C8B9 CRC64;
     MRSTKTIHVI SCHAEGEVGD VIVGGVAPPP GETLWEQRSF IARDQTLRNF VLNEPRGGVF
     RHVNLLVPPR HPEADAAFII MEPEDTPPMS GSNSICVSTV LLDGGIVPMI EPITEMVLEA
     PGGLVRVKAE CRNGKAERIF VQNVTSFADK LSVPLDVEGI GTLTVDTAYG GDSFVVVDAE
     ALGFAIVEDE AKDIARLGVR ITNAANEQLG FSHPENPDWN HISFCAFCGP LSQTPTGLTG
     RSAVAIQPGK VDRSPTGTAV SARMALMAAR GQMTIGDTFE AVSIIGSSFT GRIVSQQMAG
     DRPGIVPEIS GRGWITGIHQ HMLDPSDPWP GGYKLSDTWG A