ID A0A1Q9V2P2_9PSEU Unreviewed; 275 AA.
AC A0A1Q9V2P2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BJF85_20330 {ECO:0000313|EMBL:OLT44238.1};
OS Saccharomonospora sp. CUA-673.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=1904969 {ECO:0000313|EMBL:OLT44238.1, ECO:0000313|Proteomes:UP000186761};
RN [1] {ECO:0000313|EMBL:OLT44238.1, ECO:0000313|Proteomes:UP000186761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CUA-673 {ECO:0000313|EMBL:OLT44238.1,
RC ECO:0000313|Proteomes:UP000186761};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT44238.1}.
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DR EMBL; MKKE01000026; OLT44238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9V2P2; -.
DR STRING; 1904969.BJF85_20330; -.
DR OrthoDB; 3185659at2; -.
DR Proteomes; UP000186761; 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:InterPro.
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; 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; PTHR43580; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR PANTHER; PTHR43580:SF2; OXIDOREDUCTASE GLYR1-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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000186761}.
FT DOMAIN 1..148
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 151..266
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT REGION 255..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 275 AA; 28921 MW; 3EF16992EABB0604 CRC64;
MGLPMARNLA RAGFEVRAWN RSPDKMQPLA AEGVTLCDDV RSAAEGVDVV LTMLADADVI
LEILDDSLTR AADGAVWLQM STVGIDGTQR LADLAETAGV TFVDAPVLGT TAPAEAGELV
VLASGGEDMR ERLEPVFDAV GSRTLWVGEA GAGSRLKLVA NAWVASVVEA TAETVALAEG
LDVDPKQFLE AVSGGALDLP YLQAKATAMI ARQFDPAMKL SLAAKDTRLI DEAAADADLD
LPMLRTIRHR FAEGAREHGD DDMSATYLTS TPKAG
//
