GenomeNet

Database: UniProt
Entry: H3GCA5_PHYRM
LinkDB: H3GCA5_PHYRM
Original site: H3GCA5_PHYRM 
ID   H3GCA5_PHYRM            Unreviewed;       630 AA.
AC   H3GCA5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Class II aldolase/adducin N-terminal domain-containing protein {ECO:0000259|SMART:SM01007};
OS   Phytophthora ramorum (Sudden oak death agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra73030, ECO:0000313|Proteomes:UP000005238};
RN   [1] {ECO:0000313|Proteomes:UP000005238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
RN   [2] {ECO:0000313|EnsemblProtists:Phyra73030}
RP   IDENTIFICATION.
RC   STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra73030};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS565999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3GCA5; -.
DR   STRING; 164328.H3GCA5; -.
DR   EnsemblProtists; Phyra73030; Phyra73030; Phyra73030.
DR   VEuPathDB; FungiDB:PSURA_73030; -.
DR   eggNOG; KOG2630; Eukaryota.
DR   eggNOG; KOG2631; Eukaryota.
DR   HOGENOM; CLU_023273_3_0_1; -.
DR   InParanoid; H3GCA5; -.
DR   OMA; RNNVGRH; -.
DR   Proteomes; UP000005238; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0043874; F:acireductone synthase activity; IBA:GO_Central.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR   CDD; cd01629; HAD_EP; 1.
DR   Gene3D; 1.10.720.60; -; 1.
DR   Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   HAMAP; MF_03116; Salvage_MtnB_euk; 1.
DR   HAMAP; MF_03118; Salvage_MtnBC; 1.
DR   HAMAP; MF_03117; Salvage_MtnC_euk; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   InterPro; IPR023943; Enolase-ppase_E1.
DR   InterPro; IPR027511; ENOPH1_eukaryotes.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR   InterPro; IPR027505; MtnB_viridiplantae.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR027514; Salvage_MtnB_euk.
DR   NCBIfam; TIGR01691; enolase-ppase; 1.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   NCBIfam; TIGR03328; salvage_mtnB; 1.
DR   PANTHER; PTHR20371; ENOLASE-PHOSPHATASE E1; 1.
DR   PANTHER; PTHR20371:SF1; ENOLASE-PHOSPHATASE E1; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDF00044; enolase-phosphatase; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          153..347
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   630 AA;  69394 MW;  4A2A71799F0D4343 CRC64;
     MTPQQTSSLE LALQPTYLDS SSDCASLAVL RETGVSVDEF SASDKDGLAV DVANDEALQN
     EHSSAVDVVY NIVKGRAYLD VRDSADCWVR CTLTEGMRVA LSSHTLRRFV PVSSSAVQLL
     ESSSGARSLT PRYTRPADAA SHSTLLDANK CRELVCELCR LYYSTEWMTG TGGAMSLRHG
     ERIYVTPSGV PKERLQPKDL YVLDMDGGIL SSPKPQPGKK CPKLSDCAPL FLNAHKLRKA
     AVVLHSHGIT CNLAAALCDG KSEFRISHQE MIKGITGHGY ADTLVVPVID NAPKESALAK
     PIARAMEAHP NTAAVLVRRH GLFVWGDSWE AAKRHAECLH YLFEVAIEMR KLNLDYTVPP
     VSTSSSNGTS LKRARLDKKS NEELSMAEKH KVVMFDIEGT TTPITFVHDV LFPYVTNNVG
     RFLQQTWDKS ETQADVAGLI AQRKQDQADG VDSPAVDDQQ DKEKLIEALA AYVKWNVQAD
     RKIGPLKQLQ GHMWLQGYEN GELKALVYDD VPPCFDRLRA RGVRVGIYSS GSRQAQKLLF
     QYSDKGDLRE YLTVYFDTKI GHKREAGSYN EIVQSLGVDS GKDVLFVTDV IEEAQAAEAA
     GLDTVLSVRP GNKPLPESHH FPTIRSFAEL
//
DBGET integrated database retrieval system