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Database: UniProt
Entry: A9I3Q2_BORPD
LinkDB: A9I3Q2_BORPD
Original site: A9I3Q2_BORPD 
ID   A9I3Q2_BORPD            Unreviewed;       322 AA.
AC   A9I3Q2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=NAD-binding protein {ECO:0000313|EMBL:CAP44202.1};
GN   OrderedLocusNames=Bpet3857 {ECO:0000313|EMBL:CAP44202.1};
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:CAP44202.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP44202.1, 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).
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DR   EMBL; AM902716; CAP44202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9I3Q2; -.
DR   STRING; 94624.Bpet3857; -.
DR   KEGG; bpt:Bpet3857; -.
DR   eggNOG; COG0111; Bacteria.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd05300; 2-Hacid_dh_1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          120..296
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   322 AA;  34678 MW;  A796044D0162BE05 CRC64;
     MSAGAPLWLL CSEQEAARLA PDLAAMERDI VPCHPGDPRA VLADVAFVSR DITGRSTKFE
     IQPDTERFYA ALRAARGLRW LHVHSIGLDR EVYQEIRQRG ARVTASHGAS DAVVAQTAIA
     GVLALARQLP RLIRAQQRHA WEPLLDEHMP LDLEGQQAVV VGWGGIGQRI GQLLQALGLQ
     VSVARHSGVA AGPNVRTVPY SELGGLLPGA SWLVLACPLT DNTHGLIDAG ILAALPPHAR
     VVNVARGHVI DEPALIEALQ DRRLGGAFLD VFHHEPLPAA SPLWDMDNVI VSPHSAGFSA
     GNAARVRQIF LANLRHWLQG TL
//
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