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4HYPE_PLAL2
ID   4HYPE_PLAL2             Reviewed;         359 AA.
AC   D5SQS4;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=4-hydroxyproline 2-epimerase {ECO:0000303|PubMed:24980702};
DE            Short=4Hyp 2-epimerase;
DE            Short=4HypE {ECO:0000303|PubMed:24980702};
DE            EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN   OrderedLocusNames=Plim_2713 {ECO:0000312|EMBL:ADG68536.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetes; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290;
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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.
CC       Displays no proline racemase activity. {ECO:0000269|PubMed:24980702,
CC       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   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP001744; ADG68536.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5SQS4; -.
DR   SMR; D5SQS4; -.
DR   STRING; 521674.Plim_2713; -.
DR   EnsemblBacteria; ADG68536; ADG68536; Plim_2713.
DR   KEGG; plm:Plim_2713; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_1_0_0; -.
DR   OMA; SHVLWTG; -.
DR   OrthoDB; 559014at2; -.
DR   Proteomes; UP000002220; Chromosome.
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   Isomerase; Reference proteome.
FT   CHAIN           1..359
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432263"
FT   ACT_SITE        126
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   ACT_SITE        278
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         127..128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         279..280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   359 AA;  38173 MW;  FA0C73B97F92EAF3 CRC64;
     MTYIPRQWIQ VVDSHTGGEP TRLIYDGQHW PFAGSREGAL TSQESPSPSV LSGLRKAIDR
     SSLILPKTMS ERRQFLETEA DWLRTASLLE PRGSDVLVGA ILTPPEHASS QAGVVFCNNT
     GYLGMCGHGM IGVIVSLGQM GLIAPGPVTI DTPVGSIAAT WSGSASVTLT NVWSYRYRHA
     VSLSVPGLGV VTGDIAWGGN WFFLIGEEVH QKSLDLGNLS DLLAYTSQIR SELGRQGIAG
     AQGAEIDHVE LFASCDSSIA DSQNFVLCPG GAYDRSPCGT GTSAKLACLV ADGKVAEGGL
     WRQKSIVGSC FQAKALSIRE GERGLEVLPQ LTGEAYVTGV STLQIDEADP FRWGILPPQ
 
 
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