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3HD4E_AGRFC
ID   3HD4E_AGRFC             Reviewed;         342 AA.
AC   A9CH01;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Trans-3-hydroxy-L-proline dehydratase {ECO:0000303|PubMed:24980702};
DE            Short=T3LHyp dehydratase;
DE            Short=t3HypD {ECO:0000303|PubMed:24980702};
DE            EC=4.2.1.77 {ECO:0000269|PubMed:24980702};
DE   AltName: 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};
DE   AltName: Full=Trans-L-3-hydroxyproline dehydratase;
GN   OrderedLocusNames=Atu4684 {ECO:0000312|EMBL:AAK88766.1};
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC   STRAIN=C58 / ATCC 33970;
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 dehydration of trans-3-hydroxy-L-proline
CC       (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Can also catalyze
CC       the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-
CC       hydroxy-D-proline (c4DHyp), albeit with 30-fold lower efficiency. Is
CC       likely involved in both degradation pathways that convert t3LHyp to L-
CC       proline and t4LHyp to alpha-ketoglutarate, which would allow
CC       A.tumefaciens to grow on t3LHyp or t4LHyp as a sole carbon source.
CC       Displays no proline racemase activity. {ECO:0000269|PubMed:24980702,
CC       ECO:0000305|PubMed:24980702}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=trans-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O;
CC         Xref=Rhea:RHEA:10320, ChEBI:CHEBI:15377, ChEBI:CHEBI:39785,
CC         ChEBI:CHEBI:57938; EC=4.2.1.77;
CC         Evidence={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=2.0 mM for trans-4-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         KM=4.2 mM for trans-3-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 27 sec(-1) for t3LHyp dehydration. kcat is 0.40 sec(-1)
CC         for t4LHyp epimerization. {ECO:0000269|PubMed:24980702};
CC   -!- INDUCTION: Is up-regulated when the bacterium is grown on t4LHyp or
CC       t3LHyp as sole carbon source. {ECO:0000269|PubMed:24980702}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; AE007870; AAK88766.1; -; Genomic_DNA.
DR   PIR; AH3132; AH3132.
DR   PIR; D98155; D98155.
DR   RefSeq; NP_355981.1; NC_003063.2.
DR   RefSeq; WP_006700304.1; NC_003063.2.
DR   AlphaFoldDB; A9CH01; -.
DR   SMR; A9CH01; -.
DR   STRING; 176299.Atu4684; -.
DR   EnsemblBacteria; AAK88766; AAK88766; Atu4684.
DR   GeneID; 61458143; -.
DR   KEGG; atu:Atu4684; -.
DR   PATRIC; fig|176299.10.peg.4488; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_2_0_5; -.
DR   OMA; IMESEEY; -.
DR   PhylomeDB; A9CH01; -.
DR   BioCyc; AGRO:ATU4684-MON; -.
DR   SABIO-RK; A9CH01; -.
DR   Proteomes; UP000000813; Chromosome linear.
DR   GO; GO:0047580; F:4-hydroxyproline epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050346; F:trans-L-3-hydroxyproline dehydratase 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; Lyase; Reference proteome.
FT   CHAIN           1..342
FT                   /note="Trans-3-hydroxy-L-proline dehydratase"
FT                   /id="PRO_0000432272"
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         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT   BINDING         257..258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B9K4G4"
SQ   SEQUENCE   342 AA;  36858 MW;  8FA9CB38F0A5441A CRC64;
     MRSIKTVHVI SAHAEGEVGD VIVGGVKPPP GETIWEQSRF IARDETLRNF VLNEPRGGVF
     RHVNLLVPPK HPDADAAFII MEPEDTPPMS GSNSICVSTV LLDGGIVPMQ EPETHMLLEA
     PGGLVKVRAE CRNGKAERIF VQNLPSFAAK LDAELEVEGL GKLKVDTAYG GDSFVIVDAE
     AMGFSLKPEE AHEIARLGVR ITNAANKALG FDHPENPDWR HFSFCLFAGK VERTAEGLRA
     GAAVAIQPGK VDRSPTGTAL SARMAVLHAR GEMKEGETLT AVSLIGSTFT GRILGTTTVG
     DRPAILPEIS GRGWITGIHQ HMLDPSDPWP EGYRLTDTWG AR
 
 
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