ID A0A1Q9C4E7_SYMMI Unreviewed; 961 AA.
AC A0A1Q9C4E7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:OLP77789.1};
GN Name=GPD {ECO:0000313|EMBL:OLP77789.1};
GN ORFNames=AK812_SmicGene42113 {ECO:0000313|EMBL:OLP77789.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP77789.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP77789.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP77789.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406}.
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:OLP77789.1}.
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DR EMBL; LSRX01001712; OLP77789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9C4E7; -.
DR OrthoDB; 230345at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0016409; F:palmitoyltransferase activity; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 4.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01529; DHHC; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50216; DHHC; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 431..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 670..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..154
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT REPEAT 321..353
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 354..379
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 961 AA; 106715 MW; 02E724E1DD284765 CRC64;
MKYILWLYRV KDMKGRRDDF CRLSVQPSPN GRSEEVDGDS LVIDGQKAEL SPRVALSHTR
DPAEIPFGEH GAEYVCESTG VFLTTEKVDG DSLVIDGQKA ELSPRVALSH TRDPAEIPFG
EHGAEYVCES TGVFLTTEKD TYDPSMECVS CASCTTNGLA PAVRVLHEKF GIKRGLMTTC
HAMTASQPTV DGTSKKDWRG GRAGPGNIIP SSTGAAKAVA KVIPDVKGKL TGMALRVPTI
DVSVVDLTVE LEKDSDGNTA LHYTALFRLD SLLDPLLERG LLSMRDCDGF TAFIVAAQMD
NYLVMEWLYL KGISLEEQDD CGRTALQWAC YKGNKKTVHW LLSRSASIAH RDREGMTALH
WAVLQGHAQV VEMLMEVGAV GLIDVPDCTG ETPIALATRK KNRFLVIAFH KCQVFDFLFG
RPHVFQNLMP SAFLGFVAYH IIIFALIIAP GIAAISPEAV THWSMLMGLS LLLWVQCLFS
DPGRDPARTF DVDQPIESQM AHCDSLLQKL TLAGDGEAVE LRKLELEQNK YNYQRQLLRE
ARRRLEEACG LGNARSPAAG EMQPLITSGL NLGGSPQAQL ERATATLHEQ ERATGDSLRR
ARVEHLLAEG CGEYLRLVEN GDFKQVCVFC RIVRSMRSHH CKEQGRCVER MDHYCPWIDN
SVGLGNQRSF LLFIVVLLAT IFYFYYTVFL YAFDRVFPDI SRGELLEALT DGSLGPELQP
ILVLTTAALD LFFVLFVGSL VARTTAFMMV NLTTFEFSRR PSHVLQRFRK EGLQGATWKK
ETTYEEICAE MKNPGCRPVT HYAGNWALVS TDFETCPISC TFDSKAGIML DPTFVKDNEW
GYSCRVVDLI KPFICTSISC ASLKNIGATV VRRIHPGITG VSDFQSIAEA YEAKAQLFKM
MLETLEDDKV DAARLIQIKD GYKQTTLKVV EGAEIIRKNT IETGNIFTSQ CMGQGERLIN
T
//
