ID A0A1G2QY42_9BACT Unreviewed; 364 AA.
AC A0A1G2QY42;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN ORFNames=A2843_02590 {ECO:0000313|EMBL:OHA64912.1};
OS Candidatus Wildermuthbacteria bacterium RIFCSPHIGHO2_01_FULL_48_27b.
OC Bacteria; Candidatus Wildermuthbacteria.
OX NCBI_TaxID=1802447 {ECO:0000313|EMBL:OHA64912.1, ECO:0000313|Proteomes:UP000178170};
RN [1] {ECO:0000313|EMBL:OHA64912.1, ECO:0000313|Proteomes:UP000178170}
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:OHA64912.1}.
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; MHTS01000005; OHA64912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2QY42; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000178170; 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 Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 2.
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; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR PANTHER; PTHR11902:SF1; ENOLASE; 1.
DR Pfam; PF00113; Enolase_C; 2.
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.
DR PROSITE; PS00164; ENOLASE; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 4..116
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 123..363
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
SQ SEQUENCE 364 AA; 39893 MW; 5F4F94E8F62F376D CRC64;
MATISSLTAR KILNSRGEWT LSVELGDEHG IRVSGSAPEG ESKGTFEAEY VKPEHAVEQV
QSVVAPTLKG MDGVDQLAVD RKLVELEVGA NVSIAVSRVC ARLGAESRRM PLWKHISEIY
QTKPAAPRLF INVLEGGMHA HNNLVFQEYL AIPKANTIAR SVEIGRRVYK ALRDELKADV
GDEGGLVANF KDALEPLGLL GREADIDLGM DAAANNVDLP PAELFALYRQ MKLFYLEDPF
KENDFENFKK LKEEMGEKSI IAGDDLTTTN ITRMQKAKEE DAINGVIIKP DQIGTLTQAI
EAVSQAREWG WAVVVSHRGG ETNDDFVADL AWAVAADGLK LGGLARGERI AKYNRLLAIE
ENEA
//
