ID T5K3S4_9MICO Unreviewed; 482 AA.
AC T5K3S4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00018587, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN ORFNames=L687_03305 {ECO:0000313|EMBL:EQM74496.1};
OS Microbacterium maritypicum MF109.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1333857 {ECO:0000313|EMBL:EQM74496.1, ECO:0000313|Proteomes:UP000016033};
RN [1] {ECO:0000313|EMBL:EQM74496.1, ECO:0000313|Proteomes:UP000016033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF109 {ECO:0000313|EMBL:EQM74496.1,
RC ECO:0000313|Proteomes:UP000016033};
RX PubMed=24092793;
RA Chauhan A., Green S., Pathak A., Thomas J., Venkatramanan R.;
RT "Whole-genome sequences of five oyster-associated bacteria show potential
RT for crude oil hydrocarbon degradation.";
RL Genome Announc. 1:e00802-e00813(2013).
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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:EQM74496.1}.
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DR EMBL; ATAO01000206; EQM74496.1; -; Genomic_DNA.
DR RefSeq; WP_021200591.1; NZ_ATAO01000206.1.
DR AlphaFoldDB; T5K3S4; -.
DR PATRIC; fig|1333857.3.peg.2646; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000016033; 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; IPR018209; Pyrv_Knase_AS.
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; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 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.
DR PROSITE; PS00110; PYRUVATE_KINASE; 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:EQM74496.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016033};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EQM74496.1}.
FT DOMAIN 1..320
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 353..465
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 482 AA; 51681 MW; 2048FE21567ADC11 CRC64;
MRRAKIVATL GPATSTYETV RALIDAGVDV ARLNLSHGDY SVHENNYANV RRAAEDAGRA
VAILVDLQGP KIRLGKFENG PYELAKGDIF KITTEDIIGN KDISGTTFKG LPHDVKPGDF
LLIDDGKVRV EVVETDGVTV TTKVIVAGAV SNNKGINLPG VAVNVPALSE KDEDDLRWGL
RIGADLIALS FVRNAADVER VHEIMAEEGV RVPVIAKVEK PQAVDALEEI VDAFDAIMVA
RGDLGVELPL EAVPIVQKRA VEIARRMAKP VIVATQMLES MISSPVPTRA ETSDVANAVL
DGADAVMLSG ETSVGDYPVV VVETMARIIA STEEHGLERI APLTTKPRTQ GGAITLAALE
VAEFVDAKFL CVFTQSGDSA RRLSRLRSRI PMIAFTPEPG IRRRMALTWG IRSTLVDMVQ
HTDLMYHQVD EYLLGNGLAE EGDKVVVISG SPPGIVGSTN DLRVHKVGDA IRGAAPIYKA
GV
//
