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Database: UniProt
Entry: A0A1Q9P9P7_9ARCH
LinkDB: A0A1Q9P9P7_9ARCH
Original site: A0A1Q9P9P7_9ARCH 
ID   A0A1Q9P9P7_9ARCH        Unreviewed;       374 AA.
AC   A0A1Q9P9P7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Opine dehydrogenase {ECO:0000313|EMBL:OLS31110.1};
DE            EC=1.5.1.28 {ECO:0000313|EMBL:OLS31110.1};
GN   Name=odh {ECO:0000313|EMBL:OLS31110.1};
GN   ORFNames=HeimAB125_17200 {ECO:0000313|EMBL:OLS31110.1};
OS   Candidatus Heimdallarchaeota archaeon AB_125.
OC   Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX   NCBI_TaxID=1841596 {ECO:0000313|EMBL:OLS31110.1, ECO:0000313|Proteomes:UP000186239};
RN   [1] {ECO:0000313|EMBL:OLS31110.1, ECO:0000313|Proteomes:UP000186239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB_125 {ECO:0000313|EMBL:OLS31110.1};
RX   PubMed=28077874; DOI=10.1038/nature21031;
RA   Zaremba-Niedzwiedzka K., Caceres E.F., Saw J.H., Backstrom D.,
RA   Juzokaite L., Vancaester E., Seitz K.W., Anantharaman K., Starnawski P.,
RA   Kjeldsen K.U., Scott M.B., Nunoura T., Banfield J.F., Schramm A.,
RA   Baker B.J., Spang A., Ettema T.J.G.;
RT   "Asgard archaea illuminate the origin of eukaryotic cellular complexity.";
RL   Nature 541:353-358(2017).
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:OLS31110.1}.
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DR   EMBL; MEHH01000126; OLS31110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9P9P7; -.
DR   Proteomes; UP000186239; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0047129; F:opine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003421; Opine_DH.
DR   PANTHER; PTHR38015; BLR6086 PROTEIN; 1.
DR   PANTHER; PTHR38015:SF1; OCTOPINE_DH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   Pfam; PF02317; Octopine_DH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:OLS31110.1}.
FT   DOMAIN          3..102
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          182..324
FT                   /note="Opine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF02317"
SQ   SEQUENCE   374 AA;  41344 MW;  F97B5D92378CE3F7 CRC64;
     MTIAVIGAGC GGQAIAGYLA SKGNKVNLYN RSVDRIRPLM KKKEIELQGE IHSKGKLNLV
     TTDISEAVRG TELIMVVTTA TGHYDIATAL APHLQEEQTI ILNPGRTFGS LEFMNALLEG
     GLAADVTIAE ANTLIYATRT LRPGLSEVKG IKNSVSLSAI PNHRTSQVIS LLSEDYPQFY
     AVENFLTTSL GNIGAVFHPT ITLLNEERIR NKETFDFYRD GATREVVDYM EQVDNERRTI
     ARSFGVEVQS LKEWLCERYS LPSSNLYDAL HNNPFYAGLT APTTFDMRYL TEDIPTGLVP
     FSELGKSIGI DTRHIDNLID MASMELQVDF RSQGRNLNRL GLDARTIFED LRIVSELETI
     TEYKTAVGAI VGGD
//
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