ID   Y1705_SHEPA             Reviewed;         346 AA.
AC   A8H392;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein Spea_1705;
DE            EC=4.2.1.77 {ECO:0000269|PubMed:24980702};
GN   OrderedLocusNames=Spea_1705 {ECO:0000312|EMBL:ABV87029.1};
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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: In vitro, catalyzes the dehydration of trans-3-hydroxy-L-
CC       proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C), albeit
CC       with very low efficiency. The physiological substrate may be different.
CC       Displays neither trans-4-hydroxy-L-proline (t4LHyp) epimerase nor
CC       proline racemase activity. {ECO:0000269|PubMed:24980702, ECO:0000305}.
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         Note=kcat is 0.15 sec(-1) for t3LHyp dehydration. The reaction is too
CC         slow to measure KM for t3LHyp. {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP000851; ABV87029.1; -; Genomic_DNA.
DR   RefSeq; WP_012154949.1; NC_009901.1.
DR   AlphaFoldDB; A8H392; -.
DR   SMR; A8H392; -.
DR   STRING; 398579.Spea_1705; -.
DR   EnsemblBacteria; ABV87029; ABV87029; Spea_1705.
DR   KEGG; spl:Spea_1705; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_0_0_6; -.
DR   OMA; ERRAYCM; -.
DR   SABIO-RK; A8H392; -.
DR   Proteomes; UP000002608; 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..346
FT                   /note="Protein Spea_1705"
FT                   /id="PRO_0000432261"
FT   ACT_SITE        101
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         102..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         267..268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   346 AA;  37916 MW;  A5F1F048E98AF92A CRC64;
     MQSITITPDL SSNFKDFVTI DAHTEGEPLR VIISGYPEIK GSTILEKRQY VQQNLDTYRK
     LLMHEPRGHA DMYGALITEA VTEEADFGVL FLHNEGYSSM CGHGILALVK VMCQTDSIDL
     GLEPRTIKID SPAGLITAKA YRDSQGKIQA SFKNVDSWAD ALNCSVNVEG FGEVNYDIGF
     GGAYYAYVDA DEHGISCGQD NVAQLIDVGR RIKHAVMASH TLVHPLEEDL SFLYGTIFTS
     KKVTNPEAHS RHVCIFADGE VDRSPTGTGV SARVALLYAK GEVALNTPIM IESIVDGRMI
     VSASAESEFH GKQGVIPEVS GRSFITGKHQ FFIDPDDVFQ NGFMLR