ID F6Y110_CIOIN Unreviewed; 269 AA.
AC F6Y110;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Aspartate dehydrogenase domain-containing protein {ECO:0000256|ARBA:ARBA00020169};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000001869.2, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000001869.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008331}.
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DR AlphaFoldDB; F6Y110; -.
DR STRING; 7719.ENSCINP00000001869; -.
DR Ensembl; ENSCINT00000001869.2; ENSCINP00000001869.2; ENSCING00000001009.2.
DR GeneTree; ENSGT00390000004452; -.
DR HOGENOM; CLU_063528_0_0_1; -.
DR InParanoid; F6Y110; -.
DR OMA; HIVEVDV; -.
DR TreeFam; TF315092; -.
DR Proteomes; UP000008144; Unassembled WGS sequence.
DR GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR002811; Asp_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR31873; L-ASPARTATE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR31873:SF6; L-ASPARTATE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01958; Asp_DH_C; 1.
DR Pfam; PF03447; NAD_binding_3; 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 Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT DOMAIN 16..107
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 161..248
FT /note="Aspartate dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01958"
SQ SEQUENCE 269 AA; 28982 MW; 3C9D01ED17394F37 CRC64;
RGKMKVGIIG FGNNSKDMEL EFVWNRSKVE MEGIPEKLIL DKLEDLLKRS ADLIVEVAHP
SIAKDYGKMI LSVSDFFIGS PTALADQTTE DSLRSTALQN GRALYVPSGA FWGAQDIQKM
AQSGSLSSLK VTMKKHPSCF KLSSKKMELL NKQSIHEDRI VVLFEGSVRE LCPLAPNNVN
TMAAAAIAAS NLGFDNVVGC LVADPKMGDW HIVEIEVGGA TSANGDKFTV KTTRSNPANP
GAVTGSATFA SFRQSLLQAK NRGPGVHLC
//