ID G0SHZ2_CHATD Unreviewed; 1107 AA.
AC G0SHZ2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0000259|Pfam:PF02826};
GN ORFNames=CTHT_0073900 {ECO:0000313|EMBL:EGS17062.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS17062.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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DR EMBL; GL988048; EGS17062.1; -; Genomic_DNA.
DR RefSeq; XP_006697644.1; XM_006697581.1.
DR AlphaFoldDB; G0SHZ2; -.
DR STRING; 759272.G0SHZ2; -.
DR GeneID; 18261428; -.
DR KEGG; cthr:CTHT_0073900; -.
DR eggNOG; KOG0068; Eukaryota.
DR HOGENOM; CLU_282276_0_0_1; -.
DR OrthoDB; 2900331at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12169; PGDH_like_1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT DOMAIN 130..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 489..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 120838 MW; EF6141CC754E138B CRC64;
MVPIKVAVLD DYQGISEPKF KALDPAQFEV TFFKDTLLPY NHPDTPDEVR EQLVKRLEPF
DVISTMRERT PFPEALINRL PNLKLLLTTG TRNLSLSLPT FQARGIPVAG AVDRQHAGSV
GSVSTTEHCV AMILAAARNI AQDDLTVKNG GWQTVPAVSL KGKVFGTVGL GRLGAAVARI
MSVGFGMKVI AWSENLNQEK ADQKAREMGL PVEDTNGEKT FRAVSKEELF STADVVSIHL
VLSDRSRGCI KKRDLELMKK GAIFVNTSRG PLVVEEDLLE VLEQGRIRAA ALDVFELEPL
PANSRWRTTR WGEDGRSRVL LTPHMGYVEE ATLDAWRNRD NSEVLSIVKP IDSFPLIPLT
CIKKSPLFFG NFECLLFNKQ GDWKCQSSEN DSLVSRADPV TFSRNTGNNS SSSFTVGRSA
NSATPCIFGQ SSNEGWDRLG SLKPGEIREP SAPAAHLFSF SASPIVSHPS STAESNQLAI
GPQAQRPLQS LTASVSSPQI AHRSQTSGGT LVIGSARRQA ASTPRIIPNR VNTEAATPQL
NQRRRNTNNS AGDFTSPQIT NCSQTSSTTS SLVVTTFRAT DTSQTSGNDR VQVSAAPLIS
NVQPSLSTSK STGSTAALET SKHSQSSGSD SIQGGVTHRR SQNLNKSAAG SPATQATVRQ
SVVGLAPPQV TSLPDEVTQP TKAPALPKTN RQPMSLNKTA KAPATSGAPQ AQQTLVNKEN
NGTATPQVNQ LSPNNSNTWI GGFGTSQVDH RLQETNKAAG GSGAHQAIKS TAVKVEASNG
ESGLGRHLTQ SLPNPHAAQE EARWQARKSA LLGLSRICEF RGCIPQWETR SSNEGWFATV
IVRSTAYMAG PYRKAEWAKI VAAERALNAL GSRAFQAQKQ AQRRGSTYRP SHGKPNNNLA
ANVQQNQKSS NPTGPSSQGN MNQSQKATHQ TARPAQEQQT AHQIPHPPQQ VPINQHARPA
QHESPPHPTF PSSQHDNLAD VQLPDYARNN PIALQAFFEG LALGARMADV IIRSSREDER
SRHHERSRSR SPLQASRSDN IRRYRERTPR VSEPLRDTYR SPSESRSRRR RYRGSCLPQE
FWDRYHPASS DGANGRWEHD RYPYYDD
//
