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Database: UniProt
Entry: F6V8G3_CIOIN
LinkDB: F6V8G3_CIOIN
Original site: F6V8G3_CIOIN 
ID   F6V8G3_CIOIN            Unreviewed;       577 AA.
AC   F6V8G3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Enolase 4 {ECO:0000256|ARBA:ARBA00034855};
DE            EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|ARBA:ARBA00031125};
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:ENSCINP00000022815.2, 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:ENSCINP00000022815.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031}.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC       {ECO:0000256|ARBA:ARBA00009604}.
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DR   EMBL; EAAA01002223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; EAAA01002224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F6V8G3; -.
DR   STRING; 7719.ENSCINP00000022815; -.
DR   Ensembl; ENSCINT00000023061.2; ENSCINP00000022815.2; ENSCING00000009849.3.
DR   GeneTree; ENSGT00950000182805; -.
DR   HOGENOM; CLU_493979_0_0_1; -.
DR   InParanoid; F6V8G3; -.
DR   OMA; DIRAREC; -.
DR   TreeFam; TF354238; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000008144; Chromosome 5.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   CDD; cd22974; DD_ENO4; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   InterPro; IPR047500; DD_ENO4.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR020810; Enolase_C.
DR   PANTHER; PTHR11902; ENOLASE; 1.
DR   PANTHER; PTHR11902:SF30; ENOLASE 4; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   SMART; SM01192; Enolase_C; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT   DOMAIN          250..538
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   REGION          166..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  63340 MW;  2E79159D786A180B CRC64;
     YSYVATEALN RQSKSYQELR QNAANYYAEN AVAPKLEEIL NKMFYEQPND VYGRLSEYFE
     EFALTPNIVK ISANKVMDGV GAGGLQCSVF AEVKNQPKVL SSLSMSLEKE ISMLPLQQQH
     TTERGCMHIS ESISSKLNNV SLLQQTEVDL MLRDWIDDAE YDKFIGANQP TEEDDGHSRT
     PTPSSGRKKK TSSGKAKVGK VPEKPVPPKE PMEDRLKGCT AASAVSVAVL KAAANFLQKS
     GIAQQNVDNT VTMPTPAMVV LSGGKSAPGK LHMLKNVFAI AKPGLTISES ISNLIKVYQN
     VGKGLSAKSV NFDKIKQISA SGGYEPSYDK PEQPLDAILE AINTSGLVPG QDIFLGIECS
     AHEIFDYDKG KYEISTGTLK TADEFIDLLK DLVMRYPSLI MIIDPLRRED REQWTKLCEM
     VSEKCFIIGS DVIYGSMHSL NDNMLSARKS SGLVISTGSR VTCSDLARVV GDIRARECVT
     IMTSPVGDVC DDIFSDLAVG LGATFVRFGA PSRGENTSKI NRFIEIERII NESKTSKINY
     LSKFEFPVIK PPPPAPVSDE ENEIPAENSS PDQKKKK
//
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