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Database: UniProt
Entry: G7ZIF3_AZOL4
LinkDB: G7ZIF3_AZOL4
Original site: G7ZIF3_AZOL4 
ID   G7ZIF3_AZOL4            Unreviewed;       356 AA.
AC   G7ZIF3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative saccharopine dehydrogenase {ECO:0000313|EMBL:CBS91347.1};
DE            EC=1.5.1.- {ECO:0000313|EMBL:CBS91347.1};
GN   OrderedLocusNames=AZOLI_p50355 {ECO:0000313|EMBL:CBS91347.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p5 {ECO:0000313|EMBL:CBS91347.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS91347.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p5 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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DR   EMBL; FQ311873; CBS91347.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7ZIF3; -.
DR   KEGG; ali:AZOLI_p50355; -.
DR   HOGENOM; CLU_032858_0_0_5; -.
DR   Proteomes; UP000005667; Plasmid AZO_p5.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11133:SF22; SACCHAROPINE DEHYDROGENASE [NADP(+), L-GLUTAMATE-FORMING]-RELATED; 1.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CBS91347.1}; Plasmid {ECO:0000313|EMBL:CBS91347.1}.
FT   DOMAIN          3..98
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          120..341
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   356 AA;  38713 MW;  FE5543F760F4BA16 CRC64;
     MKVLVLGAGK IGSMIGTLLS ETEDFAVTIG DRDEALLSRA ERAGLRVTRV DVEDPSSLRA
     AMAGQHAVLS ACPFTLTPAI ATAAVAAGAH YLDLTEDVAA TRKVKLLAET ADTALIPQCG
     LAPGFISIVG HDLARRFDEL HNLHLRVGAL PQYPTNALKY NLTWSTDGLI NEYCNPCEAI
     IDGRQHEVMP LEGDERFALD GVDYEAFNTS GGLGSLCETL AGKVRNLDYK TVRYPGHRDI
     VRLLIRDLRL GERRHLLKDV LETAVPLTLQ DVVLVLATAT GMQEGELRQE TFATKIYSKP
     IAGRSWSAIQ VTTAAGICAV LDLLREGSIP QAGFIRQEQV PLDAFLNNRF GRHYRG
//
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