ID   T3HPD_BACCR             Reviewed;         334 AA.
AC   Q81HB1;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=BC_0905 {ECO:0000312|EMBL:AAP07892.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
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 allows B.cereus to grow on t3LHyp as a sole carbon source.
CC       Displays no proline racemase activity. {ECO:0000269|PubMed:24980702,
CC       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: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; AE016877; AAP07892.1; -; Genomic_DNA.
DR   RefSeq; NP_830691.1; NC_004722.1.
DR   RefSeq; WP_000868678.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81HB1; -.
DR   SMR; Q81HB1; -.
DR   STRING; 226900.BC_0905; -.
DR   PRIDE; Q81HB1; -.
DR   EnsemblBacteria; AAP07892; AAP07892; BC_0905.
DR   KEGG; bce:BC0905; -.
DR   PATRIC; fig|226900.8.peg.850; -.
DR   HOGENOM; CLU_036729_0_0_9; -.
DR   OMA; ERRAYCM; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0047580; F:4-hydroxyproline epimerase activity; IBA:GO_Central.
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..334
FT                   /note="Trans-3-hydroxy-L-proline dehydratase"
FT                   /id="PRO_0000432267"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         92..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         255..256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   334 AA;  36840 MW;  9789F3E4640D9BD2 CRC64;
     MKVSKIYTTI DAHVAGEPLR IITGGVPEIK GETQLERRAY CMEHLDYLRE ILMYEPRGHH
     GMYGCIITPP ASAHADFGVL FMHNEGWSTM CGHGIIAVIT VGIETGMFEV TGEKQKFIID
     SPAGEVIAYA TYSGSEVESV SFENVPSFVY KKDVPIKIDS YEFQVDIAFG GAFYAVVDSK
     EFGLKVDFKD LSAIQMWGGK IKHYIESKME VKHPLEEGLK GIYGVIFSDD PKEKDATLRN
     VTIFADGQVD RSPCGTGTSA RIATLFAKDA LQKGEIFVHE CITDGKFEGE VLSVTAVHTY
     EAVVPKVTGN AFITGFHQFV VDPRDDLNRG FLLG