ID   A0A093Q2K7_9PASS        Unreviewed;       928 AA.
AC   A0A093Q2K7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFW83193.1};
GN   ORFNames=N305_10867 {ECO:0000313|EMBL:KFW83193.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW83193.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW83193.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW83193.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) 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}.
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DR   EMBL; KL671658; KFW83193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093Q2K7; -.
DR   STRING; 328815.ENSMVIP00005002565; -.
DR   UniPathway; UPA00868; UER00835.
DR   Proteomes; UP000053258; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053258}.
FT   DOMAIN          28..158
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          198..400
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   928 AA;  103386 MW;  406280F878E51F3B CRC64;
     MLRAFSHTNG RCMFHHTKCW HHRKSVLAIR REDVNAWERR APLAPKHVKE LTKMGYKVLV
     QPSNRRAIHE KEYIKAGAII QEDISEASLI IGVKRPPEEK LIPKKNYAFF SHTIKAQEAN
     MPLLDEILRQ EIRLFDYEKM VDHKGMRVVA FGKWAGVAGM INILHGLGLR FLALGHHTPF
     MHIGMAHNYR NSSQAVQAVR DAGYEISLGL MPKSVGPLTF VFTGTGNVSK GAQEMFNALP
     CEFVEPHELK EVSRSGDLRK VYGTVLSRHH HLVRKHDGIY DPVDYEKHPE NYTSRFHIDV
     APYTTCLING IYWEQHTPRL LSRQDAQKLL VPVISADGST EGCPELPHKL LAICDISADT
     GGSIEFMTEC TTIENPFCMY DADQHITHDS VEGSGILMCS IDNLPAQLPI EATEYFGDML
     FPYIEEMLSS EGSEPLEKQN YSPVVRDAVI ASNGSLTPKY QYIQKLRESR EQAQSLKMGE
     KKRVLLLGSG YVSGPVLEYL TRDSNIGITV VSVMKEQLEQ LTKKYNNVTS VHMDVLKREE
     KLSSLVKKHD LVISLLPYSA HPFVAKKCIE NKVNLVTASY LTPAMKELQE SVEAAGITVV
     SEMGLDPGLD HMLAMECIDK AKEVGATVIS YTSFCGGLPA PEHSDNPLRY KFSWSPQGVL
     LNTVQSATYL KDGEIINIPA GGALLDSVTP MDFFPGLNLE GFPNRDSTKY AEPYGIQTAR
     TLLRGTLRYK GYSKTMGGFV KLGLINPDPY PLLSSTTPPL TWKELMCKLV GIKSPVEHHV
     LKEAVFSKLE KDKSQLEAVE WLGLLGDEQV PAADSIVGAL AKHMEMKLPF GTGERDMIIM
     RNEIGLRHPS GHLEDKFVDL VVYGDNKGHS AMAKTVGYPT AIAAKMVLDG EIVAKGMVIP
     LTKNVYGPIL ERVRAEGIVY STHSVIKQ
//