4HPE2_BRUA4
ID 4HPE2_BRUA4 Reviewed; 337 AA.
AC A6WXX7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=4-hydroxyproline 2-epimerase 2 {ECO:0000303|PubMed:24980702};
DE Short=4Hyp 2-epimerase 2;
DE Short=4HypE 2 {ECO:0000303|PubMed:24980702};
DE EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN OrderedLocusNames=Oant_1111 {ECO:0000312|EMBL:ABS13831.1};
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 epimerization of trans-4-hydroxy-L-proline
CC (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a
CC degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can
CC also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp)
CC to cis-3-hydroxy-D-proline (c3DHyp), albeit with 170-fold lower
CC efficiency. Displays no proline racemase activity.
CC {ECO:0000269|PubMed:24980702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline;
CC Xref=Rhea:RHEA:21152, ChEBI:CHEBI:57690, ChEBI:CHEBI:58375;
CC EC=5.1.1.8; Evidence={ECO:0000269|PubMed:24980702};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC KM=31 mM for trans-3-hydroxy-L-proline {ECO:0000269|PubMed:24980702};
CC Note=kcat is 89 sec(-1) for t4LHyp epimerization. kcat is 2.4 sec(-1)
CC for t3LHyp epimerization. {ECO:0000269|PubMed:24980702};
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; CP000758; ABS13831.1; -; Genomic_DNA.
DR RefSeq; WP_012091266.1; NC_009667.1.
DR AlphaFoldDB; A6WXX7; -.
DR SMR; A6WXX7; -.
DR STRING; 439375.Oant_1111; -.
DR EnsemblBacteria; ABS13831; ABS13831; Oant_1111.
DR KEGG; oan:Oant_1111; -.
DR PATRIC; fig|439375.7.peg.1161; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_0_0_5; -.
DR OMA; SHVLWTG; -.
DR OrthoDB; 559014at2; -.
DR PhylomeDB; A6WXX7; -.
DR SABIO-RK; A6WXX7; -.
DR Proteomes; UP000002301; Chromosome 1.
DR GO; GO:0047580; F:4-hydroxyproline epimerase 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 Isomerase; Reference proteome.
FT CHAIN 1..337
FT /note="4-hydroxyproline 2-epimerase 2"
FT /id="PRO_0000432277"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT ACT_SITE 253
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 254..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ SEQUENCE 337 AA; 37252 MW; 9B1F82ED21F0A528 CRC64;
MARHSFFCVD GHTCGNPVRL VAGGGPNLEG STMMEKRAHF LREYDWIRTG LMFEPRGHDM
MSGSILYPPT RPDCDVAVLF IETSGCLPMC GHGTIGTVTM AIEQGLVTPK TPGKLNLDTP
AGLVAIEYEQ NGQYVERVRL TNVPAFLYAE GLEVECPDLG NLKVDVAYGG NFYAIVEPQE
NYTDMEDYSA LQLIAWSPIL RERLNEKYKF QHPLLPDINR LSHILWTGKP KHPEAHARNA
VFYGDKAIDR SPCGTGTSAR MAQLAAKGKL KPGDEFVHES IIGSLFHGRV ERATEVVGQD
RTLPAIIPSI AGWARMTGYN TIFIDDRDPF AHGFTVA
