ID A0A1M6FQB9_9CLOT Unreviewed; 222 AA.
AC A0A1M6FQB9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN ORFNames=SAMN02745975_01053 {ECO:0000313|EMBL:SHI99887.1};
OS Geosporobacter subterraneus DSM 17957.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Geosporobacter.
OX NCBI_TaxID=1121919 {ECO:0000313|EMBL:SHI99887.1, ECO:0000313|Proteomes:UP000184536};
RN [1] {ECO:0000313|EMBL:SHI99887.1, ECO:0000313|Proteomes:UP000184536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17957 {ECO:0000313|EMBL:SHI99887.1,
RC ECO:0000313|Proteomes:UP000184536};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}.
CC -!- SIMILARITY: Belongs to the enolase family.
CC {ECO:0000256|ARBA:ARBA00009604}.
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DR EMBL; FQZV01000012; SHI99887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6FQB9; -.
DR STRING; 1121919.SAMN02745975_01053; -.
DR OrthoDB; 9804716at2; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000184536; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR PANTHER; PTHR11902:SF1; ENOLASE; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR PRINTS; PR00148; ENOLASE.
DR SMART; SM01192; Enolase_C; 1.
DR SUPFAM; SSF51604; Enolase C-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 Pyruvate {ECO:0000313|EMBL:SHI99887.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 2..220
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
SQ SEQUENCE 222 AA; 24680 MW; 3FC15D77908C2448 CRC64;
MAEPRFLLGL LQALQLIVEA IGRAKYTPGE DVMIALDPAA SEFFVDGQYN LAGQGVKMNS
KELLAYYEYL ISNYPIISIE DGFHEEDWEA FAEMTKKLGN KIQVMGDDIY VTNPVRLQRG
IQENTTNSIL IKLNQIGTLS ETLDTIQMAH RAGYTTVVSH RSGETEDTTI SELVVAINAG
QIKTGAPARS ERVAKYNQLL RIEEQLGMAS IYPGVKCLYN LK
//
