T3HPD_SACKO
ID T3HPD_SACKO Reviewed; 326 AA.
AC P0DKB4;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Trans-L-3-hydroxyproline dehydratase;
DE EC=4.2.1.77;
DE AltName: Full=Trans-3-hydroxy-L-proline dehydratase;
GN Name=l3hypdh;
OS Saccoglossus kowalevskii (Acorn worm).
OC Eukaryota; Metazoa; Hemichordata; Enteropneusta; Harrimaniidae;
OC Saccoglossus.
OX NCBI_TaxID=10224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Qu J., Zhang L., Abraham K.K., Akbar H., Ali S., Alvi O., Anosike U.S.,
RA Aqrawi P.K., Archer P.M., Arias F., Arredondo H.H., Attaway T., Babu C.,
RA Bachman B., Bandaranaike D.P., Barton M.L., Battles P.K., Bell A.V.,
RA Bell S.N., Berhane-Mersha D., Bess C.M., Bickham C., Blyth P.R.,
RA Bolden T.M., Bonnen P.E., Bourquin T., Buhay J.C., Canada A., Cardenas V.,
RA Carter K., Carter A.J., Chaboub L., Chacko J., Chandrabose M.N., Chang K.,
RA Chavez D., Chavez A., Chen R., Chen G., Chen D., Chu H.,
RA Clerc Blankenburg K.P., Cockrell R., Collier R.T., Coyle M.D., Cree A.,
RA Curry S.M., Dao M.D., Davila M., Davy-Carroll L., Deiros D.R., Demen R.,
RA Deng J., Denson S., Dilber J.M., Ding Y., Dinh H.H., Drabek R.B., Du A.,
RA Dugan-Rocha S., Dunn A.M., Durbin K.J., Ebong V.E., Elkadir S.,
RA Espinosa V.C., Fernandez S., Fernando P.R., Ferrer A.R., Finley M.C.,
RA Flagg N., Forbes L.D., Fowler R.G., Francis C.S., Fu Q., Gabisi R.A.,
RA Ganer J., Garcia S.M., Garcia R.M., Garner T.T., Garrett T.E., Gingras M.,
RA Goodell J., Gross S., Gubbala S., Guevara W.V., Gurugunti A., Hale W.,
RA Hall O., Hamid H., Han Y., Harbes B.A., Havlak P., Hawes A.C.,
RA Hawkins E.S., Haynes S.J., Hernandez J., Hines S., Hirani K.,
RA Hitchens M.E., Hogues M.E., Holder M., Hollins B., Hume J., Igboeli O.C.,
RA Jackson L.R., Jacob S.K., Jakkamsetti A., Jhangiani S.N., Jiang H.,
RA Jing C., Johnson A.J., Johnson B., Jones J., Joshi V., Joy C., Kalu J.B.,
RA Khan N.R., Khan Z.M., Kidwai S., Kisamo H., Kovar C.L., Kowis A.N.,
RA Lago M.T., Lago L.A., Lai C., Lara F., Latif Z.A., Le T.T., Leal B.,
RA Lee S.L., Legall F.H., Lemon S.J., Lewis L.R., Li Z., Liu Y., Liu W.,
RA Liu J., Liu X., Liu Y., Liyanage D., London P., Lopez J., Lorensuhewa L.M.,
RA Lozado R.J., Lu Y., Madu R.C., Malloy K., Martinez E., Mathew T.,
RA McPherson J.D., Mercado I.C., Mercado C., Metcalf G.A., Metzker M.L.,
RA Milosavljevic A., Moen C., Morales K.R., Morgan M.B., Mulakkamparambath A.,
RA Munidasa M., Murray D.D., Nazareth L.V., Ng B.M., Ngo D.N., Nguyen T.S.,
RA Nguyen L., Nguyen P.Q., Nwaokelemeh O.O., Obregon M., Okwuonu K.C.,
RA Onwere C.G., Osuji N., Padilla R., Parker D.N., Parra S.A., Pasternak S.,
RA Patel R.R., Patel B.M., Patil S.S., Perez L., Perez A., Perez Y.Y.,
RA Pham P.A., Pham T.L., Primus E.L., Pu L., Puazo M., Qin X., Quiroz J.B.,
RA Rabata D., Rachlin E.K., Raj R.A., Reid J.G., Ren Y., Robinson T.,
RA Rojas A., Rouhana J., Ruiz S., Ruiz M.J., Saada N., Sabo A., San Lucas F.,
RA Santibanez J., Savery G.G., Scheel M., Scherer S.E., Schneider B.W.,
RA Shen Y., Shen H., Sisson I.O., Skiles W.J., Sodergren E., Song X., Song B.,
RA Tang L., Thelus R.A., Thomas N., Thorn R.D., Thornton R.D., Tisius J.R.,
RA Toledanes G., Tombrello J., Trejos Z.Y., Usmani K., Varghese R.T.,
RA Vattathil S., Vee V., Villasana D., Walker D.L., Wang S., Wang Q.,
RA Warren J.T., Watt J.E., Wei X., Weissenberger G.M., Wheeler D.A.,
RA White C.S., Wilczek-Boney K.B., Williams G.J., Williams G.A.,
RA Williams A.C., Williams R.E., Wilson K.C., Woghiren I.O., Wright R.A.,
RA Xi L., Xin Y., Yao J., Zhang J., Zhao Z., Zhou J., Zhou C., Zhu D., Zhu Y.,
RA Muzny D.M., Richards S., Weinstock G., Worley K.C., Gibbs R.A.;
RT "Genome Sequence of Acorn Worm (Saccoglossus kowalevskii).";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22528483; DOI=10.1074/jbc.m112.363218;
RA Visser W.F., Verhoeven-Duif N.M., de Koning T.J.;
RT "Identification of a human trans-3-Hydroxy-L-proline dehydratase, the first
RT characterized member of a novel family of proline racemase-like enzymes.";
RL J. Biol. Chem. 287:21654-21662(2012).
CC -!- FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline to
CC delta-1-pyrroline-2-carboxylate (Pyr2C). {ECO:0000269|PubMed:22528483}.
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:22528483};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast to the T.cruzi proline racemase enzyme,
CC lacks the conserved Cys at position 245 which is replaced by a Thr
CC residue, transforming the racemase activity into dehydratase activity.
CC {ECO:0000250}.
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; ACQM01021026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DKB4; -.
DR SMR; P0DKB4; -.
DR PRIDE; P0DKB4; -.
DR OrthoDB; 894373at2759; -.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
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.
FT CHAIN 1..326
FT /note="Trans-L-3-hydroxyproline dehydratase"
FT /id="PRO_0000419462"
FT ACT_SITE 80
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 81..82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246..247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 36078 MW; 6536F280DBBC8436 CRC64;
MHTGGEPLRI VTDGFPKPDG KTILQKRRFV KEKLDNFRKL LMHEPRGHYD MYGALLVEPD
IEDADIAVLF MDNRSYSTMC GHAVIALGRY ATDYGYVRPT EPETKVNIEC PCGLVKALVE
YKNGKSGSVR FQSVPAFVFA TDVELNVQGH GKVKVDISYG GAFYAFISAD KLGLDLWKTP
INQIKDAATM VTNAVKNEVQ LEHPDDNDLA FIYGTIVTDG KDEYSDEPTA NICVFADAQV
DRSPTGSGVT ARTALQYHKR HISLNKSRVF VNARIGSKFS AKPVRQTKCG SYDAVIIEVS
GHAFYTGKSA FTFEEDDPLK GGFLLK
