ID A0A3S3PQ54_9ACAR Unreviewed; 957 AA.
AC A0A3S3PQ54;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Alpha-aminoadipic semialdehyde synthase-like protein {ECO:0000313|EMBL:RWS14242.1};
GN ORFNames=B4U79_02839 {ECO:0000313|EMBL:RWS12986.1}, B4U79_03849
GN {ECO:0000313|EMBL:RWS12979.1}, B4U79_08941
GN {ECO:0000313|EMBL:RWS13658.1}, B4U79_11149
GN {ECO:0000313|EMBL:RWS14242.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS14242.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS14242.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS14242.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:RWS14242.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS14242.1};
RA Dong X.;
RT "Trombidioid mite genomics.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC {ECO:0000256|ARBA:ARBA00004682}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC {ECO:0000256|ARBA:ARBA00004720}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00025744}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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:RWS14242.1}.
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DR EMBL; NCKU01001143; RWS12979.1; -; Genomic_DNA.
DR EMBL; NCKU01001142; RWS12986.1; -; Genomic_DNA.
DR EMBL; NCKU01000925; RWS13658.1; -; Genomic_DNA.
DR EMBL; NCKU01000768; RWS14242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3PQ54; -.
DR STRING; 1965070.A0A3S3PQ54; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000285301; Unassembled WGS sequence.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR CDD; cd12189; LKR_SDH_like; 1.
DR Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301}.
FT DOMAIN 59..189
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 229..432
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 957 AA; 106319 MW; 9BF1B3E4F4A7A46A CRC64;
MIWKVTVPAV KLLCHSPESI VQKCSPKWTS FHIFKRLKGT YHYSKSRPSI SYDGAKTLAI
RREDASIWER RAPLAPSHVR KLTKRGVRVL VQPSNRRAYP SQAYVNAGAV IQEDISDSPV
IIGVKQVPID SLLPNKTYVF FSHTIKAQED NMPMLDAILE RNVRLIDYEK MVGSNGQRVV
AFGRYAGIAG MINILHGLGL RLLALGHHTP FMHIGPAHNY RNSGMARQAV RDCGYEIALG
MMPRSIGPLT VVLTGSGNVS QGAQEILQEL PYEYVDPKDL PQVSQMGSTN KVYASVVSRD
DHLFRKDGGR FDMEEFEQHP DRYYSNFATA IAPFASIIIN GIYWAVSSPR ILTIPDMKRI
MQPQNTPWLP SSVGSPSLPH RLLAICDISA DPGGSIEFMT ECTTIDTPFC LYDADYNKQS
EKFSGPGVLV CSIDNMPTQL PLEATEAFGD MLFPYIDDII NSEANKPFEE ERMHPVVKGA
VIASNGKLTP NFEYIMDLRR MRATEAAGEK STSILVLGAG YVSSPLVEYL TRDQSLHVTV
ASALHGQGEA VANKSSNTSS LVLDVTKRPE QLDELISKSD LVISLLPYHF HPMVAKKCIE
QKKNMITASY ASPEMKALHS AACEAGITIV NEVGLDPGID HLLAMECFDQ VTSNGGKITS
FVSYCGGLPA PEHADNPLGY KFSWNPRSVL LNCLKSARWL ENGEVKEIPD GGVLMDNAAE
VDFLRAFNLE GYPNRDSLIY KDMYGITNAH TVLRGTLRYR GFCDNMKCLL KMGLLDTKPH
PSLHPKGPEI TWKQFMCTLL GQKEDILPIN LRNLVLERVE GHESRLAALE TLGLLDDKLI
EKLGSPFETL TNYLAQRLAF RGKEQDLVIM RHNIGIEWPN GSKEVRDINL VVYGDPNGYS
AMAKTVGYPA AIAAKMLLEE EIQKRGIVLP MTTEIYSPML KRLQKEGICS IEKSTKL
//
