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Database: UniProt
Entry: Q7W9Z2_BORPA
LinkDB: Q7W9Z2_BORPA
Original site: Q7W9Z2_BORPA 
ID   Q7W9Z2_BORPA            Unreviewed;       374 AA.
AC   Q7W9Z2;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Racemase {ECO:0000313|EMBL:CAE36907.1};
GN   OrderedLocusNames=BPP1606 {ECO:0000313|EMBL:CAE36907.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|EMBL:CAE36907.1, ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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DR   EMBL; BX640427; CAE36907.1; -; Genomic_DNA.
DR   RefSeq; WP_010928111.1; NC_002928.3.
DR   AlphaFoldDB; Q7W9Z2; -.
DR   GeneID; 69420983; -.
DR   KEGG; bpa:BPP1606; -.
DR   HOGENOM; CLU_030273_3_1_4; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProt.
DR   CDD; cd03316; MR_like; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   InterPro; IPR046945; RHMD-like.
DR   PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR   PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDG00179; mandelate_racemase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          149..247
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   374 AA;  41742 MW;  EE9637A803E2B42E CRC64;
     MAIIKSIEVC VARVPMDKVT YLSNRTVVDR HYGLVKVRSA DGVEGIGFCY VGNQAGEIFR
     VAVEQLLGPV LIGRDSLAVE GLWREMYQEA LLQGRMGTVM RALSALDIAL WDLNARAANL
     PLHKYLGAVE LDSVAAYASG GYYVEGKTAG QLGEEMASYV ELGFKAVKMK TGRWSPQGEQ
     SRVRAAREAI GEDVELMLDC NNGWVDTVQA MEYLRRMEPY NPYFIEEPFS PDDVESHARL
     ARLTRIPVAT AEIGYGRWYH KQLLDMGAAA ILQTDAAVCG GITEWKRIAA MAAGYGIQMC
     PHWFHDVHAP LAAATPNARY VEFFWDDQVL NFRRLVDRQL EHKDGRVILH QTPGLGFGFD
     ENAVARYGRW TTES
//
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