C3HPD_ROSAI
ID C3HPD_ROSAI Reviewed; 367 AA.
AC A0NXQ8;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Cis-3-hydroxy-L-proline dehydratase {ECO:0000303|PubMed:25608448};
DE Short=c3LHyp dehydratase {ECO:0000303|PubMed:25608448};
DE Short=c3LHypD {ECO:0000303|PubMed:25608448};
DE EC=4.2.1.171 {ECO:0000269|PubMed:25608448};
GN ORFNames=SIAM614_28497 {ECO:0000312|EMBL:EAV42585.1};
OS Roseibium aggregatum (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC
OS 16684 / NCIMB 2208 / IAM 12614 / B1) (Stappia aggregata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Roseibium.
OX NCBI_TaxID=384765;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM
RC 12614 / B1;
RA King G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, MUTAGENESIS OF LYS-165 AND LYS-265, INDUCTION, AND ACTIVE SITE.
RC STRAIN=ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM
RC 12614 / B1;
RX PubMed=25608448; DOI=10.1021/ja5103986;
RA Zhang X., Kumar R., Vetting M.W., Zhao S., Jacobson M.P., Almo S.C.,
RA Gerlt J.A.;
RT "A unique cis-3-hydroxy-L-proline dehydratase in the enolase superfamily.";
RL J. Am. Chem. Soc. 137:1388-1391(2015).
CC -!- FUNCTION: Catalyzes the dehydration of cis-3-hydroxy-L-proline (c3LHyp)
CC to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a
CC degradation pathway that converts c3LHyp to L-proline, which allows
CC L.aggregata to grow on c3LHyp as a sole carbon source. Also catalyzes
CC the epimerization of c3LHyp to trans-3-hydroxy-D-proline (t3DHyp), a
CC competing reaction occurring from the same enolate anion intermediate.
CC L-proline, t3LHyp, t4LHyp, c4DHyp and their methylated derivatives are
CC not substrates. {ECO:0000269|PubMed:25608448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cis-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O;
CC Xref=Rhea:RHEA:47624, ChEBI:CHEBI:15377, ChEBI:CHEBI:39785,
CC ChEBI:CHEBI:60041; EC=4.2.1.171;
CC Evidence={ECO:0000269|PubMed:25608448};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25608448};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:25608448};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.1 mM for cis-3-hydroxy-L-proline {ECO:0000269|PubMed:25608448};
CC Note=kcat is 14 sec(-1) for c3LHyp epimerization, and 9 sec(-1) for
CC c3LHyp dehydration. {ECO:0000269|PubMed:25608448};
CC -!- INDUCTION: Is up-regulated when the bacterium is grown on c3LHyp or
CC t3LHyp as sole carbon source. {ECO:0000269|PubMed:25608448}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; AAUW01000014; EAV42585.1; -; Genomic_DNA.
DR RefSeq; WP_006937105.1; NZ_AAUW01000014.1.
DR PDB; 4MGG; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-367.
DR PDBsum; 4MGG; -.
DR AlphaFoldDB; A0NXQ8; -.
DR SMR; A0NXQ8; -.
DR KEGG; ag:EAV42585; -.
DR eggNOG; COG4948; Bacteria.
DR OrthoDB; 951991at2; -.
DR BRENDA; 4.2.1.171; 9995.
DR Proteomes; UP000004848; Unassembled WGS sequence.
DR GO; GO:0016597; F:amino acid binding; IDA:UniProtKB.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IDA:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR034620; Cis-3-h-L-Pro_dehydratase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00555; cis-3-hydroxy-L-proline_dehydr; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..367
FT /note="Cis-3-hydroxy-L-proline dehydratase"
FT /id="PRO_0000433398"
FT ACT_SITE 165
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:25608448"
FT ACT_SITE 265
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:25608448"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25608448,
FT ECO:0007744|PDB:4MGG"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25608448,
FT ECO:0007744|PDB:4MGG"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25608448,
FT ECO:0007744|PDB:4MGG"
FT MUTAGEN 165
FT /note="K->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:25608448"
FT MUTAGEN 265
FT /note="K->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:25608448"
FT STRAND 3..15
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 27..40
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4MGG"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 99..117
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:4MGG"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:4MGG"
FT TURN 266..270
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 298..309
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:4MGG"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:4MGG"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:4MGG"
SQ SEQUENCE 367 AA; 39636 MW; 68AD95D7E34CD4BB CRC64;
MKITAINVFQ VDLPLREGRY SWSNGNFVEV FDSTVVEIET DEGLKGYAEC CPLGSAYLPS
YALGVRSGLQ ELAPHLIGKD PLNIGEINRV MDAALRGHPY AKAPIDIACW DLLGKATGQP
LYTLLGGAAQ DDVALYRAIS QEAPEIMAKK IEGYAAEGYT KFQLKVGGDA NDDINRIHAT
RSVLKKSDLL VADANTGWTR HEAARVVGAV SSLDVYIEQP CLTYEESVSI RRRTALPFVL
DEVIDGPNTL VRGIAEDAMD CINLKISKVG GLTKAKLMRD LCIAHGIPMT IEDTWGGDIV
TAAIAHLARS TPSEFTFSAT DFNSYGTVDI AEGAPKRVNG RMTTSDLPGL GITPIFDVLG
EPVARYS
