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Database: UniProt
Entry: A0A1B9NGJ1_9MICO
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ID   A0A1B9NGJ1_9MICO        Unreviewed;       481 AA.
AC   A0A1B9NGJ1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   Name=pyk {ECO:0000313|EMBL:QBR74124.1};
GN   ORFNames=A7J15_01370 {ECO:0000313|EMBL:OCG75729.1}, E3O41_06625
GN   {ECO:0000313|EMBL:QBR74124.1};
OS   Microbacterium sediminis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=904291 {ECO:0000313|EMBL:OCG75729.1, ECO:0000313|Proteomes:UP000093355};
RN   [1] {ECO:0000313|EMBL:OCG75729.1, ECO:0000313|Proteomes:UP000093355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLB-01 {ECO:0000313|EMBL:OCG75729.1,
RC   ECO:0000313|Proteomes:UP000093355};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QBR74124.1, ECO:0000313|Proteomes:UP000295661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLB-01 {ECO:0000313|EMBL:QBR74124.1,
RC   ECO:0000313|Proteomes:UP000295661};
RA   Yu L.;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QBR74124.1, ECO:0000313|Proteomes:UP000295661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLB-01 {ECO:0000313|EMBL:QBR74124.1,
RC   ECO:0000313|Proteomes:UP000295661};
RA   Xu X.;
RT   "Genomic analysis of Microbacterium sediminis YLB-01 reveals backgrounds
RT   related to its deep sea enviroment adaptation.";
RL   Submitted (APR-2019) 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   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
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; LXMD01000012; OCG75729.1; -; Genomic_DNA.
DR   EMBL; CP038256; QBR74124.1; -; Genomic_DNA.
DR   RefSeq; WP_067023239.1; NZ_KV744781.1.
DR   AlphaFoldDB; A0A1B9NGJ1; -.
DR   STRING; 904291.A7J15_01370; -.
DR   KEGG; msed:E3O41_06625; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000093355; Unassembled WGS sequence.
DR   Proteomes; UP000295661; 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; 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: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.
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:OCG75729.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093355};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:QBR74124.1}.
FT   DOMAIN          1..322
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          354..465
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   481 AA;  51793 MW;  5936699DDE8D7108 CRC64;
     MRRAKIVATL GPATSTQETV KELIEAGVDV TRFNLSHGDY SVHDNNYANV RAAAEEVGKP
     VAVLVDLQGP KIRLGKFADG PHELAVGDIF KITIEDIPGT KEIVSTTFKG LPADVKPGDF
     LLIDDGKVRV KVIQSDDTVV TTEVVVAGTV SNNKGINLPG VAVNVPALSE KDEADLRWGL
     RKGADLIALS FVRDAKDIQR VHVIMAEEGR FVPVIAKIEK PQAVDHLEEI IEAFDGIMVA
     RGDLGVELPL EAVPIVQKTA VEIARRLAKP VIVATQMLES MIESPVPTRA ETSDVANAVI
     DGADAVMLSG ETSVGAYPVV TVQTMARIIE STEEHGLERI HPITNRPRTQ GGIITLAAVE
     VADFVEAKYL CIFTEGGDSA RRMARLRSRI PMIAFTTDEA IRRRMALTWG IRSALVDPVD
     HTDRMFIQVD DYLLANDLAK VGDKVVVISG SPPGISGSTN DIRIHKVGDA VHGAAPVYQQ
     G
//
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