ID A0A151XEM7_9HYME Unreviewed; 436 AA.
AC A0A151XEM7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Enolase {ECO:0000256|ARBA:ARBA00017068};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|ARBA:ARBA00031125};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000256|ARBA:ARBA00032132};
GN ORFNames=ALC60_02171 {ECO:0000313|EMBL:KYQ58833.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ58833.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ58833.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ58833.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ58833.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; KQ982249; KYQ58833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151XEM7; -.
DR STRING; 64791.A0A151XEM7; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR PANTHER; PTHR11902:SF1; ENOLASE; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809}.
FT DOMAIN 3..134
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 142..433
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
SQ SEQUENCE 436 AA; 48558 MW; CD6326508C5F5826 CRC64;
MALRKIKARQ IFDSRGEPTL EVDVITDIGL FRSSVPSTVL PNPNQAREIR DENKMAYHGR
SVFKVVNIIN NVIAPQLIKS RLEVCQQTEI DELLNKLDGT ENKSRLGVNA ILGVSVACCK
AGAAKKGLPV YRYIAELAEN NKLCIPVPSF SMINGGRYAG NNLSYQEFMI LPVGAESFAD
ALKMATEMYR VLERNIIDAK QIRRPLLIND NGAFAPDLEN DEAALTLLDA SIRDAGYEGK
IKIALDVAAS AFYKEGKYDL AFKTKDSDPT NYLEAEALRD QYLRYLSKFP AIFSIKDPFA
QEDWNGWLMI AHQGIQVVSD DLTAMNIERI EEAMNRNIAN CLVLRISQIG TVTEVINCAR
MAIINNWNYI VSASHGETED NFIADLAVGL SAGQFIAGAP CRSERIGKYN QILRIEEELG
KDAKYIGTKY QNPLMK
//
