ID A0A1P8UEN8_9GAMM Unreviewed; 479 AA.
AC A0A1P8UEN8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
GN ORFNames=BW247_03820 {ECO:0000313|EMBL:APZ42323.1};
OS Acidihalobacter ferrooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Acidihalobacter.
OX NCBI_TaxID=1765967 {ECO:0000313|EMBL:APZ42323.1, ECO:0000313|Proteomes:UP000243807};
RN [1] {ECO:0000313|EMBL:APZ42323.1, ECO:0000313|Proteomes:UP000243807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V8 {ECO:0000313|EMBL:APZ42323.1,
RC ECO:0000313|Proteomes:UP000243807};
RA Khaleque H.N., Ramsay J.P., Murphy R.J.T., Kaksonen A.H., Boxall N.J.,
RA Watkin E.L.J.;
RT "Draft sequence of Acidihalobacter ferrooxidans strain DSM 14175 (strain
RT V8).";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000256|RuleBase:RU000504};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; CP019434; APZ42323.1; -; Genomic_DNA.
DR RefSeq; WP_076835855.1; NZ_CP019434.1.
DR AlphaFoldDB; A0A1P8UEN8; -.
DR STRING; 1765967.BW247_03820; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000243807; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:APZ42323.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243807};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 8..329
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 364..472
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 479 AA; 52027 MW; D1D03D384AADD02A CRC64;
MPATLASHKT KIVCTIGPAS AKPAVLARMI RAGMNVARIN LAHGDPHSHT ATIARVREAA
AQAGRDVAIL ADLPGPKLRI GTLSPDPLRL HHGQRFTLTT EDVPGTVERV SVPDFAELPQ
AVRAGESIFL NDGFIQLKVL EIAGPEVRCR VTVGGELRSH KGLNIPHMHI RLPAFTERDQ
SLLAFACEQQ VDAVSISFVE NAADIERVRR EAVALGAAPL LIAKIERADA LTHFDEILAA
ADGCMVARGD LGVETPIEAI ALVQKRLIRK ANARCKPVIT ATQMLESMVD HSRPTRAEAT
DVANAVLDGT DAVMLSEESA IGTYPVEAVK MLGRIARQAE AARGEHARAP VLDDRRNARH
SIEDTISLNV VTAVGHLRAA YVFTPTETGA TARRIARFHL PTWTIALSRH DATCRRLLFS
YGVHPVHTAE DARDWRDIAY HWMRENSLVG DPLIFTLGTS RGHPGTTNRV EILPGIGRR
//
