Y1586_BRUME
ID Y1586_BRUME Reviewed; 342 AA.
AC Q8YFD6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein BMEI1586;
DE EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN OrderedLocusNames=BMEI1586;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN [2]
RP LACK OF ENZYMATIC ACTIVITY AS PROLINE RACEMASE AND HYDROXYPROLINE
RP 2-EPIMERASE.
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=17849014; DOI=10.1371/journal.pone.0000885;
RA Goytia M., Chamond N., Cosson A., Coatnoan N., Hermant D., Berneman A.,
RA Minoprio P.;
RT "Molecular and structural discrimination of proline racemase and
RT hydroxyproline-2-epimerase from nosocomial and bacterial pathogens.";
RL PLoS ONE 2:E885-E885(2007).
RN [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=17588214; DOI=10.1007/s10969-007-9018-3;
RA Forouhar F., Kuzin A., Seetharaman J., Lee I., Zhou W., Abashidze M.,
RA Chen Y., Yong W., Janjua H., Fang Y., Wang D., Cunningham K., Xiao R.,
RA Acton T.B., Pichersky E., Klessig D.F., Porter C.W., Montelione G.T.,
RA Tong L.;
RT "Functional insights from structural genomics.";
RL J. Struct. Funct. Genomics 8:37-44(2007).
CC -!- FUNCTION: In vitro, catalyzes the epimerization of trans-4-hydroxy-L-
CC proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) and that of trans-
CC 3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp),
CC albeit with very low efficiency. The physiological substrate may be
CC different (PubMed:24980702). Displays neither proline racemase activity
CC nor t3LHyp dehydratase activity (PubMed:17849014, PubMed:24980702).
CC {ECO:0000269|PubMed:17849014, ECO:0000269|PubMed:24980702,
CC ECO:0000305|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=4.5 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC KM=2.6 mM for trans-3-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC Note=kcat is 0.082 sec(-1) for t4LHyp epimerization. kcat is 0.085
CC sec(-1) for t3LHyp epimerization. {ECO:0000269|PubMed:24980702};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17588214}.
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; AE008917; AAL52767.1; -; Genomic_DNA.
DR PIR; AD3450; AD3450.
DR RefSeq; WP_004682925.1; NZ_GG703778.1.
DR PDB; 1TM0; X-ray; 2.80 A; A/B=1-342.
DR PDBsum; 1TM0; -.
DR AlphaFoldDB; Q8YFD6; -.
DR SMR; Q8YFD6; -.
DR STRING; 224914.BMEI1586; -.
DR EnsemblBacteria; AAL52767; AAL52767; BMEI1586.
DR GeneID; 29594445; -.
DR KEGG; bme:BMEI1586; -.
DR PATRIC; fig|224914.52.peg.2003; -.
DR eggNOG; COG3938; Bacteria.
DR OMA; IMESEEY; -.
DR PhylomeDB; Q8YFD6; -.
DR SABIO-RK; Q8YFD6; -.
DR EvolutionaryTrace; Q8YFD6; -.
DR Proteomes; UP000000419; Chromosome I.
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.
FT CHAIN 1..342
FT /note="Protein BMEI1586"
FT /id="PRO_0000354042"
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 7..14
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1TM0"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1TM0"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:1TM0"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1TM0"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 158..178
FT /evidence="ECO:0007829|PDB:1TM0"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1TM0"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:1TM0"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:1TM0"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:1TM0"
SQ SEQUENCE 342 AA; 36974 MW; FB6E5E9208EF98DC CRC64;
MRSTKVIHIV GCHAEGEVGD VIVGGVAPPP GETVWEQSRF IANDETLRNF VLNKPRGGVF
RHVNLLVPPK DPRAQMGFII MEPADTPPMS GSNSICVSTV LLDSGIIAMQ EPVTHMVLEA
PGGIIEVEAE CRNGKAERIS VRNVPSFADR LDAPLDVTGL GTIMVDTAYG GDSFVIVDAA
QIGMKIEPGQ ARELAEIGVK ITKAANEQLG FRHPERDWRH ISFCQITEPV TREGDVLTGV
NTVAIRPAKF DRSPTGTGCS ARMAVLHAKG QMKAGERFIG KSVLGTEFHC RLDKVLELGG
KPAISPIISG RAWVTGTSQL MLDPSDPFPH GYRLSDTWPR DE
