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Database: UniProt
Entry: A9I5A0_BORPD
LinkDB: A9I5A0_BORPD
Original site: A9I5A0_BORPD 
ID   A9I5A0_BORPD            Unreviewed;       272 AA.
AC   A9I5A0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Aldolase {ECO:0000313|EMBL:CAP41077.1};
GN   OrderedLocusNames=Bpet0745 {ECO:0000313|EMBL:CAP41077.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP41077.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP41077.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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DR   EMBL; AM902716; CAP41077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9I5A0; -.
DR   STRING; 94624.Bpet0745; -.
DR   KEGG; bpt:Bpet0745; -.
DR   eggNOG; COG3836; Bacteria.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR   PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          33..250
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   272 AA;  27620 MW;  7DBAED78DB213B11 CRC64;
     MSRATPCAHS ALKARLARGE LAMSLIVRSA RGPEIALVAR SSGFDALYID LEHSPLSLDT
     ASMLCIASQA AGVTPLVRVP QASAAWVSRA LDGGAMGVIV PHVEDAATAR AAVALAKYPP
     LGQRSVSTTL PQLAYQAMPA AESQCLLNRE TLVVAMIESR QGLWHADEIA AVEGIDMLLV
     GAGDLAADLG AAGPAVQAAL RDAFDTVIAA CKRHGKAAGA GGLAGQLDLL AEVVAAGVRY
     VSAGTDTGFL LAGAQAKVAA IRARCPPGAD GR
//
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