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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//