ID N8QEY0_9GAMM Unreviewed; 290 AA.
AC N8QEY0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=F994_01481 {ECO:0000313|EMBL:ENU20422.1};
OS Acinetobacter bohemicus ANC 3994.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217715 {ECO:0000313|EMBL:ENU20422.1, ECO:0000313|Proteomes:UP000013086};
RN [1] {ECO:0000313|EMBL:ENU20422.1, ECO:0000313|Proteomes:UP000013086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 3994 {ECO:0000313|EMBL:ENU20422.1,
RC ECO:0000313|Proteomes:UP000013086};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. ANC 3994.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HIBADH-related family.
CC {ECO:0000256|ARBA:ARBA00009080}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENU20422.1}.
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DR EMBL; APOH01000011; ENU20422.1; -; Genomic_DNA.
DR RefSeq; WP_004651841.1; NZ_KB849176.1.
DR AlphaFoldDB; N8QEY0; -.
DR PATRIC; fig|1217715.3.peg.1439; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_1_6; -.
DR OrthoDB; 9786703at2; -.
DR Proteomes; UP000013086; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF15; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 5..157
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 160..281
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 290 AA; 30756 MW; CD4C95032C62F81C CRC64;
MIQSVAFIGL GAMGYRMAAH LPQHFDTVYV WNRNFEKAKQ HATEYGTQAV ELAQAVQADV
IFSCLPTSKD VEELIASVKI KSGSIWVDCT SGVPESAKTL ATQLKLHNID FLDAPVSGQT
IGAETATLTV MVGGEAAGFE KALPAMQAFG KLIKHVGGSG AGFSVKAVNN MLLAVNLCSV
AEGFTALKAH GVNLHEALDC INASSGKSGV TETVLPQRIL NRSFPLTFAL PLLAKDTGIA
LDLVREAKLS APVIALTQSL IQASSDLSEK DSDFSSAVKM YESWSKITLE
//