ID A0A0D8FYA1_9ACTN Unreviewed; 491 AA.
AC A0A0D8FYA1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN Name=pyk {ECO:0000313|EMBL:KJE77959.1};
GN ORFNames=FEAC_03310 {ECO:0000313|EMBL:KJE77959.1};
OS Ferrimicrobium acidiphilum DSM 19497.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Ferrimicrobium.
OX NCBI_TaxID=1121877 {ECO:0000313|EMBL:KJE77959.1, ECO:0000313|Proteomes:UP000032336};
RN [1] {ECO:0000313|EMBL:KJE77959.1, ECO:0000313|Proteomes:UP000032336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T23 {ECO:0000313|EMBL:KJE77959.1,
RC ECO:0000313|Proteomes:UP000032336};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Ferrimicrobium acidiphilum
RT strain T23.";
RL Submitted (JAN-2015) 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}.
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:KJE77959.1}.
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DR EMBL; JXUW01000002; KJE77959.1; -; Genomic_DNA.
DR RefSeq; WP_052565187.1; NZ_JXUW01000002.1.
DR AlphaFoldDB; A0A0D8FYA1; -.
DR STRING; 1121877.FEAC_03310; -.
DR GeneID; 78371673; -.
DR PATRIC; fig|1121877.4.peg.362; -.
DR eggNOG; COG0469; Bacteria.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000032336; Unassembled WGS sequence.
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:KJE77959.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032336};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:KJE77959.1}.
FT DOMAIN 5..328
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 362..474
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 491 AA; 52100 MW; 854699BA5F7107F8 CRC64;
MNAPRRTKIV CSIGPASQEV DSLVALIEAG MNVARVNMSH GTFAEHSTTI DNVREAARRT
GQIIGILGDL CGPKLRITGL PARIHLVKPG DQFMLSEGDP EEDVDAITIT PLGVLTEVAR
GDSIAFADGA VRGLVQERNE HGVSVLVTQG GSLSIRKGVN LPDSHLSIPA MTDKDFHDAS
FLLEHNVDFL ALSFVGSASD LTIAREFMLE NAHGPNIPRL VAKIERRDAL GRIAEIMDVA
DAVMVARGDL GVEIPVEEVP IEQKRIIHLA NARGKMVITA TQMLESMISA PTPTRAEASD
VANAILDGTD AIMLSAETAV GSYPVDAVGQ MDRIARATEQ IVTDQSLTLL THPVRAIHST
ADAIGFAAAD LSRNLALKVV IAVTESGHSA RTISRYRPNV PVVGATPDEF AARSLTLSYG
VIPAVIPRSP STEVMIQEAI DAAIDLDLCE TGDLCALAAG IPFGVRGTTN LVKIQVVGEG
FLSIGDRYQT D
//
