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T3HPD_AGRVS
ID   T3HPD_AGRVS             Reviewed;         342 AA.
AC   B9K4G4;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Avi_7022 {ECO:0000312|EMBL:ACM39762.1};
OS   Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain
OS   S4)).
OG   Plasmid pAtS4e {ECO:0000312|EMBL:ACM39762.1,
OG   ECO:0000312|Proteomes:UP000001596}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=311402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 / ATCC BAA-846;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PYRROLE
RP   2-CARBOXYLATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND ACTIVE SITE.
RC   STRAIN=S4 / ATCC BAA-846;
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       Displays neither proline racemase activity nor 4-hydroxyproline 2-
CC       epimerase 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         KM=15 mM for trans-3-hydroxy-L-proline {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 4.3 sec(-1) for t3LHyp dehydration.
CC         {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP000638; ACM39762.1; -; Genomic_DNA.
DR   RefSeq; WP_015918209.1; NC_011981.1.
DR   PDB; 4K7G; X-ray; 2.00 A; B/D=1-342.
DR   PDBsum; 4K7G; -.
DR   AlphaFoldDB; B9K4G4; -.
DR   SMR; B9K4G4; -.
DR   STRING; 311402.Avi_7022; -.
DR   EnsemblBacteria; ACM39762; ACM39762; Avi_7022.
DR   KEGG; avi:Avi_7022; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_2_0_5; -.
DR   OMA; IMESEEY; -.
DR   OrthoDB; 559014at2; -.
DR   SABIO-RK; B9K4G4; -.
DR   Proteomes; UP000001596; Plasmid pAtS4e.
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   3D-structure; Lyase; Plasmid; Reference proteome.
FT   CHAIN           1..342
FT                   /note="Trans-3-hydroxy-L-proline dehydratase"
FT                   /id="PRO_0000432250"
FT   ACT_SITE        90
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:24980702"
FT   BINDING         91..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:24980702"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:24980702"
FT   BINDING         257..258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:24980702"
FT   STRAND          7..14
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          20..25
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   HELIX           34..44
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   HELIX           46..52
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   HELIX           91..103
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          111..120
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          123..132
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          135..142
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          146..157
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   TURN            158..160
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          161..178
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   TURN            180..183
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   HELIX           191..208
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          224..228
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          232..234
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          237..246
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   TURN            247..249
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   HELIX           257..269
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          279..282
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          288..299
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          302..311
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   STRAND          313..321
FT                   /evidence="ECO:0007829|PDB:4K7G"
FT   TURN            336..338
FT                   /evidence="ECO:0007829|PDB:4K7G"
SQ   SEQUENCE   342 AA;  36363 MW;  67E15D7878ABF529 CRC64;
     MRTNKVIHVI GVHAEGEVGD VIVGGVSPPP GDTLWEQSRF IASDETLRNF VLNEPRGGVF
     RHVNLLVPPK DPRAQMGFII MEPADTPPMS GSNSICVSTA ILDSGIISMQ EPLTHMVLEA
     PGGVIEVTAE CANGKAERIN VLNVASFVTR LAAALEVEGL GTLTVDTAYG GDSFVIVDAI
     GLGFSLKPDE ARELAELGMK ITAAANEQLG FVHPCNADWN HISFCQMTTP ITRENGILTG
     KSAVAIRPGK IDRSPTGTGC SARLAVMHAR GEIGIGETYI GRSIIDSEFK CHIDSLTEIG
     GLSAIRPVIS GRAWITGVSQ LMLDPTDPWP SGYQLSDTWP AI
 
 
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