ID   T3HPD_COLP3             Reviewed;         355 AA.
AC   Q485S0;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Trans-3-hydroxy-L-proline dehydratase {ECO:0000303|PubMed:24649405};
DE            Short=T3LHyp dehydratase {ECO:0000303|PubMed:24649405};
DE            Short=t3HypD;
DE            EC=4.2.1.77 {ECO:0000269|PubMed:24649405};
DE   AltName: Full=Trans-L-3-hydroxyproline dehydratase;
GN   Name=lhpH {ECO:0000303|PubMed:24649405};
GN   OrderedLocusNames=CPS_1453 {ECO:0000312|EMBL:AAZ23960.1};
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=24649405; DOI=10.1016/j.fob.2014.02.010;
RA   Watanabe S., Tanimoto Y., Yamauchi S., Tozawa Y., Sawayama S., Watanabe Y.;
RT   "Identification and characterization of trans-3-hydroxy-L-proline
RT   dehydratase and Delta(1)-pyrroline-2-carboxylate reductase involved in
RT   trans-3-hydroxy-L-proline metabolism of bacteria.";
RL   FEBS Open Bio 4:240-250(2014).
CC   -!- FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline
CC       (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Together with
CC       LhpI, is involved in a metabolic pathway that converts t3LHyp to L-
CC       proline. {ECO:0000269|PubMed:24649405}.
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:24649405};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0-9.5. {ECO:0000269|PubMed:24649405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24649405}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000083; AAZ23960.1; -; Genomic_DNA.
DR   RefSeq; WP_011042289.1; NC_003910.7.
DR   AlphaFoldDB; Q485S0; -.
DR   SMR; Q485S0; -.
DR   STRING; 167879.CPS_1453; -.
DR   EnsemblBacteria; AAZ23960; AAZ23960; CPS_1453.
DR   KEGG; cps:CPS_1453; -.
DR   HOGENOM; CLU_036729_0_0_6; -.
DR   OMA; ERRAYCM; -.
DR   OrthoDB; 559014at2; -.
DR   BRENDA; 1.5.1.49; 8143.
DR   BRENDA; 4.2.1.77; 8143.
DR   Proteomes; UP000000547; Chromosome.
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..355
FT                   /note="Trans-3-hydroxy-L-proline dehydratase"
FT                   /id="PRO_0000432242"
FT   ACT_SITE        111
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         112..113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         276..277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   355 AA;  38956 MW;  32927595A4571A4F CRC64;
     MTKNIAQAAV KFEQWQPKIE QESYLTINSL ECHTGGEPLR IITSGFPVLK GNTILAKAND
     CKQNYDQLRR ALMFEPRGHA DMYGAIITDA ERDDSHFGAV FIHNEGYSSM CGHAVIALTK
     TAVESGVVAR TGDVTQVVID VPCGQIYAMA YSHNNVVKHV SFQCVPSFVY AKDQQVEVDG
     IGMVQFDIAY GGAFYAYVQA SSLGLSLVPE QQEKLIAYGR KIKQAIIPQF EINHPTTAEL
     SFLYGVIFID DSPNQDVHSR NVCIFADGEL DRSPTGSGVS GRIALHHAKQ QIVLNETITI
     ESILASSFSV RAIETVCFAG FDAVIPEVTG DAYVCGKGQW FINAEDPLKY GFLLR