4HPE1_BRUA4
ID 4HPE1_BRUA4 Reviewed; 343 AA.
AC A6WW16;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=4-hydroxyproline 2-epimerase 1 {ECO:0000303|PubMed:24980702};
DE Short=4Hyp 2-epimerase 1;
DE Short=4HypE 1 {ECO:0000303|PubMed:24980702};
DE EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN OrderedLocusNames=Oant_0439 {ECO:0000312|EMBL:ABS13170.1};
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 X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP 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) in vitro, albeit with low
CC efficiency. The physiological substrate may be different. Displays no
CC proline racemase activity. {ECO:0000269|PubMed:24980702, ECO:0000305}.
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=1.3 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC Note=kcat is 0.064 sec(-1) for t4LHyp epimerization.
CC {ECO:0000269|PubMed:24980702};
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; CP000758; ABS13170.1; -; Genomic_DNA.
DR RefSeq; WP_012090731.1; NC_009667.1.
DR PDB; 4K8L; X-ray; 1.90 A; A=1-343.
DR PDBsum; 4K8L; -.
DR AlphaFoldDB; A6WW16; -.
DR SMR; A6WW16; -.
DR STRING; 439375.Oant_0439; -.
DR EnsemblBacteria; ABS13170; ABS13170; Oant_0439.
DR KEGG; oan:Oant_0439; -.
DR PATRIC; fig|439375.7.peg.468; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_2_0_5; -.
DR OMA; IMESEEY; -.
DR OrthoDB; 559014at2; -.
DR PhylomeDB; A6WW16; -.
DR SABIO-RK; A6WW16; -.
DR Proteomes; UP000002301; Chromosome 1.
DR GO; GO:0047580; F:4-hydroxyproline epimerase 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 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..343
FT /note="4-hydroxyproline 2-epimerase 1"
FT /id="PRO_0000432248"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:4K8L"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:4K8L"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4K8L"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 146..156
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 162..179
FT /evidence="ECO:0007829|PDB:4K8L"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:4K8L"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:4K8L"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:4K8L"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:4K8L"
SQ SEQUENCE 343 AA; 36899 MW; ADE36139FF040D81 CRC64;
MRSTKVIHIV GCHAEGEVGD VIVGGVAPPP GKTVWEQSRF IASDETLRNF VLNEPRGGVF
RHVNLLVPPK DPRAQMGFII MEPADTPPMS GSNSICVSTV LLDSGIIPMQ EPVTRMVLEA
PGGLIEVEAE CRNGKAERIS VRNVPSFADR LNASLEVEGL GTITVDTAYG GDSFVIVDAA
SIGMKIEPGQ ARELAEIGVK ITKAANEQLG FRHPEKDWNH ISFCQITEPV TRDGDILTGV
NTVAIRPAKL DRSPTGTGCS ARMAVLHAKG QMKVGERFIG KSVLGTEFHC RLDKTLELGG
KPAISPIISG RAWVTGTSQL MLDPSDPFPS GYRLSDTWPN MPE
