ID A0A0F4YGY6_TALEM Unreviewed; 858 AA.
AC A0A0F4YGY6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0000256|ARBA:ARBA00012991};
DE EC=1.1.1.31 {ECO:0000256|ARBA:ARBA00012991};
GN ORFNames=T310_9517 {ECO:0000313|EMBL:KKA16903.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA16903.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA16903.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA16903.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-
CC oxopropanoate + H(+) + NADH; Xref=Rhea:RHEA:17681, ChEBI:CHEBI:11805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57700,
CC ChEBI:CHEBI:57945; EC=1.1.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00000062};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000256|ARBA:ARBA00005109}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00006013}.
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:KKA16903.1}.
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DR EMBL; LASV01000732; KKA16903.1; -; Genomic_DNA.
DR RefSeq; XP_013323515.1; XM_013468061.1.
DR AlphaFoldDB; A0A0F4YGY6; -.
DR STRING; 1408163.A0A0F4YGY6; -.
DR GeneID; 25321450; -.
DR OrthoDB; 203032at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd07730; metallo-hydrolase-like_MBL-fold; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR22981:SF7; 3-HYDROXYISOBUTYRATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22981; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Branched-chain amino acid catabolism {ECO:0000256|ARBA:ARBA00022456};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT DOMAIN 121..149
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF00753"
FT DOMAIN 515..704
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 710..832
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
SQ SEQUENCE 858 AA; 94459 MW; A87CF1AD57710828 CRC64;
MATAIPFPPP PSSDPHVYVT ISALEGGHLT LPEKLFVTDA DPDKRSTVPS LSFLIQHPNK
QNENQNQNQK SGFDKIVFDL GIKRDLSAYH PAMHSHIANR QPVLTRPDVA DSLRQGGLDP
ASDIDYVILS HVHWDHVGTP GDFLQATFVL GPGTLRLLEQ GAPPHYPKEI FDSGMLPRER
VWEMPCTSSP GSTSSKEDGY VGDKARAFQG REWRPLCTSS NDSGNEILFP AVIDLFNDSS
LYLIDSPGHL YGHMNLLARI GPTKWVYLGG DCCHDPRILT GEKDIALYDD GRGGLRSVHV
DTDGARRTLE RIRRFTNNQR GGLDGSVEIE IEVIVAHDAV WRERNRHRFF SEEVVIISVL
QMYRINNNTL FRSVPYFPAF SPTVGFALTI DIHHLPKSGK PQPHRRSIVG NMTSFLASQL
DYRGEDTNQL GRNIYLGRYS REFNFSPRHR PRQYMYLCMD LLQRNILYST LPYLIIINRV
KENNGNGYSR QDDRVHRYAD TSSILISLHS TYLSICLGVM GYPMAINLRT KLGPEYKLLI
CDVSSDALHK FQDEMQEKKT GPVEVVANGF EAVKAADLVI TMLPGTPAVQ AVYLDPSTGI
LAGVKDAAAA AADSPRRKII MECGTIETAT ILEVARATKD TASALSSGWT LTFVDAPVSG
GPMGAQAGTL TFMVGVDSAS NANNHTFNAV KSVLSHMGKA ENIFLCGEVG AGTAFKIINN
YLSAITSLAA SEALNIGVKM GLDPKLLTDV INTSGGQCWV TSKSNPVPGV QDNVPSSRNY
EGGFRIELCK KVLGMGSQLA EMVGARTILD KPTLAAFEEA AADPRYAGKD ARVVYKWLNE
SIRTYLIYLQ VDISNNQM
//
