C3HPD_STAND
ID C3HPD_STAND Reviewed; 367 AA.
AC D7A0Y2;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
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 OrderedLocusNames=Snov_0156 {ECO:0000312|EMBL:ADH87492.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Starkeya.
OX NCBI_TaxID=639283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456;
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456;
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). May be involved in a
CC degradation pathway that converts c3LHyp to L-proline, which would
CC allow S.novella to grow on c3LHyp as a sole carbon source.
CC {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:0000250|UniProtKB:A0NXQ8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:A0NXQ8};
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; CP002026; ADH87492.1; -; Genomic_DNA.
DR RefSeq; WP_013164997.1; NC_014217.1.
DR AlphaFoldDB; D7A0Y2; -.
DR SMR; D7A0Y2; -.
DR STRING; 639283.Snov_0156; -.
DR EnsemblBacteria; ADH87492; ADH87492; Snov_0156.
DR KEGG; sno:Snov_0156; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_4_5_5; -.
DR OMA; GRQDEWF; -.
DR OrthoDB; 951991at2; -.
DR Proteomes; UP000006633; Chromosome.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; 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 Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..367
FT /note="Cis-3-hydroxy-L-proline dehydratase"
FT /id="PRO_0000433399"
FT ACT_SITE 165
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0NXQ8"
FT ACT_SITE 265
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0NXQ8"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A0NXQ8"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A0NXQ8"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A0NXQ8"
SQ SEQUENCE 367 AA; 39340 MW; 78AA8484278DDCCC CRC64;
MKITGIKAWK VGLPLKEGRY NWSNGNFVEV FDSTVVAVET DAGITGYAEC CPLGSAYLPA
YAHGVRAGLE EIGPKVIGLD PTDLNVLNRH MDSVLRGHPY VKAPIDIACW DILGKVSGLP
VYKLLGGAAQ EKVALYRAIS QEAPEAMARK IAGYKAEGYT KFQLKVGGDA DQDIDRIRVT
REILDATDTL VADANTGWTR AEAARIAAEV GDLDVYIEQP CPTYEECLSV RARTARPFVL
DEVIDGVGTL MKALADDAMD IINLKISKVG GLTKARLMRD ICVASGTPMT IEDTWGGDIV
TATIAHLARS TPEEFSFSAT DFNSYGTVDI AKGAPKRVNG FMTASDAPGL GIEPIFEVLG
EPVVVIG
