ID A0A182RK59_ANOFN Unreviewed; 930 AA.
AC A0A182RK59;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AFUN006627-PA};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN006627-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN006627-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN006627-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A182RK59; -.
DR STRING; 62324.A0A182RK59; -.
DR EnsemblMetazoa; AFUN006627-RA; AFUN006627-PA; AFUN006627.
DR VEuPathDB; VectorBase:AFUN006627; -.
DR VEuPathDB; VectorBase:AFUN2_001291; -.
DR OrthoDB; 2184985at2759; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000075900; 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; 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}.
FT DOMAIN 27..157
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 197..400
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 930 AA; 102752 MW; 8A2BF150D2B5E1C9 CRC64;
MFRILKCSEH LSVRQFTRGK HTGKVIAIRR EDQSVWERRA SFPPAVVKKL IKQGVKVIVQ
PSNRRAYPMQ AYLNAGATVQ EDISEASVIF GVKQVPVDAL IPQKTYCFFS HTIKAQESNM
PLLDACLEKN IRLVDYEKLM DRNGLRLVAF GKYAGVAGMV NILHGLGLRL LALGHHTPFM
HVGPAHNYRN SSMARQAVRD CGYEISLGMM PKSIGPLTFI FTGSGNVSQG AQEVFQELPV
EFVPPEMLRK VAEHGSTNKL YGCEVSRSDH LERREGGKFD PVEYDQYPER YISTFSNNIA
PYASVIVNGI YWAVGAPKLI TIPDAKNLLR PANTPWLPTS RGSPALPHRM LAICDISVDP
GGSIEFMNEC TTIDTPFCLY DADRNKDQKS FKGPGVLVCS IDNMPTQLPR EATDFFGDLL
YPYALDILQS DASKPLAEHN FCQPVEGAII CSNGSLTPGY EYINELRELN SRSRHKTEGC
YEGKKRVLVL GAGFVSAPLV EYLHRESNVS IKVASQYKEE ADRLAHRYQG VESVYVNVQD
ESANLQNLCE ESDVVVSLLP YSLHSVIAKH CIAGKTHLVT ASYVNDDINA LHSAAQDAGV
TIMNEVGLDP GIDHLLALEC IQDVQENGGV VESFVSFCGG LPAPEHSDNP LRYKFSWSPR
GVLLNTLSAA KYLSKGQVVE ITGGGELMSA PRELEFLPGF ALEGFPNRDS TKYQSLYGLT
NINTLLRGTI RYKGFSDTIK PMQLLGLIDP NPHPLLHPHG PELTWRQLIV NMLGLADADI
FIENLKYKLA ERVGTIEGLE ELGLLENAPV VKMGSPLDTL SYYLSKKLAF ADTERDLVVL
RHDVGIRWSD GRREERGINF VVYGQPASQG GHSAMAKTVG FPAAIAAKMI IDGEIQQRGV
VLPFSADIYR PMLARLEQEG LTATTTTKVL
//
