ID A0A1G0VLV7_9BACT Unreviewed; 308 AA.
AC A0A1G0VLV7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE Flags: Fragment;
GN ORFNames=A2330_11195 {ECO:0000313|EMBL:OGV10151.1};
OS Ignavibacteria bacterium RIFOXYB2_FULL_36_7.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798447 {ECO:0000313|EMBL:OGV10151.1, ECO:0000313|Proteomes:UP000176959};
RN [1] {ECO:0000313|EMBL:OGV10151.1, ECO:0000313|Proteomes:UP000176959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGV10151.1}.
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DR EMBL; MHAT01000072; OGV10151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0VLV7; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000176959; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 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 NCBIfam; TIGR01060; eno; 1.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR PANTHER; PTHR11902:SF1; ENOLASE; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 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 Pyruvate {ECO:0000313|EMBL:OGV10151.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 4..134
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 139..308
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT NON_TER 308
FT /evidence="ECO:0000313|EMBL:OGV10151.1"
SQ SEQUENCE 308 AA; 33211 MW; C7D80F266E927334 CRC64;
MTTIVDVFAR EILDSRGNPT LESEVELESG AIGRAAVPSG ASTGEHEAVE LRDGDKSRYL
GKGVLKAVEN VNEKICSELV ELDAADQASI DSLLIELDGT KNKGNLGANA MLGVSLACAR
AVAQTLGMPL YRYIGGTNAK TLPVPMMNIL NGGKHADNNV DFQEFMIMPV GAPNFAEALR
MGSETFHALK SVLSKKGYNT AVGDEGGFAP NLKSNEEAID VILEAVNKAG YKIKDEIAIA
LDPAASEFYI KDKDAYHLFK SAPDKIIPKE KMVDFWADWA SKYPIVSIED GLAEDDWDGW
LLLTQKLG
//
