ID C3ZUH3_BRAFL Unreviewed; 445 AA.
AC C3ZUH3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=trans-L-3-hydroxyproline dehydratase {ECO:0000256|ARBA:ARBA00013105};
DE EC=4.2.1.77 {ECO:0000256|ARBA:ARBA00013105};
GN ORFNames=BRAFLDRAFT_92246 {ECO:0000313|EMBL:EEN43812.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN43812.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN43812.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN43812.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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:0000256|ARBA:ARBA00001148};
CC -!- SIMILARITY: Belongs to the proline racemase family.
CC {ECO:0000256|ARBA:ARBA00007529}.
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DR EMBL; GG666683; EEN43812.1; -; Genomic_DNA.
DR RefSeq; XP_002587801.1; XM_002587755.1.
DR AlphaFoldDB; C3ZUH3; -.
DR STRING; 7739.C3ZUH3; -.
DR eggNOG; ENOG502QRPF; Eukaryota.
DR InParanoid; C3ZUH3; -.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0050346; F:trans-L-3-hydroxyproline dehydratase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008794; Pro_racemase_fam.
DR PANTHER; PTHR33442; TRANS-3-HYDROXY-L-PROLINE DEHYDRATASE; 1.
DR PANTHER; PTHR33442:SF1; TRANS-3-HYDROXY-L-PROLINE DEHYDRATASE; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF05544; Pro_racemase; 1.
DR SFLD; SFLDS00028; Proline_Racemase; 1.
DR SUPFAM; SSF54506; Diaminopimelate epimerase-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 3: Inferred from homology;
FT DOMAIN 252..361
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 367..444
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 407..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 48599 MW; C482C83FD405AFD6 CRC64;
MADPKRQVTI SDSKPPPFVI KTVEMHTGGE PVRIITNGYP KIEGKTILEK RAYVRDHLDV
FRKRLLWEPR GHYDMYGALL VEPDDKTADI GVLFMHNKGY GTMCGHACIR LGRYVVDKGI
VAATSPRTEV VIQCPTGPVK MWVDCEDGKS GRVRFHSVPA FVFALDQEVD VPNYGRVKVD
IASGGAFYAF LPDSSLGLDL RTAPIEAVRS AAIAVTEAVK KAVPLRHPEH PEMAYLDGTI
ITDGRDEYDQ TPTLQTSVFG GFFVDRSPCG SGTTARVAIL TVVLRCAFDQ LAEEDDVIWD
GPDFKVISYG SKVLRVYNRH HIMGDAARGE FNLEIRQAQL EDDGKYSCYT DPKAAASALL
TVVVPMPTPP TITGGELMVT AGEQLSLTCR ASGGHPAARL TWLNGTRSLR SESQTTENLP
SQRSGCHPNH GLFLGPTAPS SKVSN
//
