T3HPD_BACHK
ID T3HPD_BACHK Reviewed; 334 AA.
AC Q6HMS9;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Name=prdF {ECO:0000312|EMBL:AAT62415.1};
GN OrderedLocusNames=BT9727_0799 {ECO:0000312|EMBL:AAT62415.1};
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 Can also catalyze the epimerization of trans-4-hydroxy-L-proline
CC (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) in vitro. Displays no
CC 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.5 mM for trans-3-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC Note=kcat is 23 sec(-1) for t3LHyp dehydration. kcat is 0.16 sec(-1)
CC for t4LHyp epimerization. The reaction of t4LHyp epimerization is too
CC slow to measure KM for t4LHyp. {ECO:0000269|PubMed:24980702};
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; AE017355; AAT62415.1; -; Genomic_DNA.
DR RefSeq; YP_035142.1; NC_005957.1.
DR AlphaFoldDB; Q6HMS9; -.
DR SMR; Q6HMS9; -.
DR EnsemblBacteria; AAT62415; AAT62415; BT9727_0799.
DR KEGG; btk:BT9727_0799; -.
DR PATRIC; fig|281309.8.peg.835; -.
DR HOGENOM; CLU_036729_0_0_9; -.
DR OMA; ERRAYCM; -.
DR SABIO-RK; Q6HMS9; -.
DR Proteomes; UP000001301; Chromosome.
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..334
FT /note="Trans-3-hydroxy-L-proline dehydratase"
FT /id="PRO_0000432269"
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; 36841 MW; C51F840031F9AB30 CRC64;
MKVSKVYTTI DAHVAGEPLR IITGGVPEIK GDTQLERRAY CMEHLDHLRE VLMYEPRGHH
GMYGCIITPP ASAHADFGVL FMHNEGWSTM CGHGIIAVIT VGIETGMFEV TGEKQNFIID
SPAGEVIAYA KYNGSEVESV SFENVPSFVY KKDVPIIIDD YEFQVDIAFG GAFYAVVDSK
EFGLKVDFKD LSAIQMWGGK IKHYIESKME VKHPLEEGLK GIYGVIFSDE PKGEDATLRN
VTIFADGQVD RSPCGTGTSA RIATLFEKDA LQKGEIFVHE CITDGKFEGE VLSVTAVDTY
EAVVPKVTGH AFITGFHQFV VDPRDDLKRG FLLG
