ID A0A1G8SKY8_9NOCA Unreviewed; 599 AA.
AC A0A1G8SKY8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN ORFNames=SAMN05444695_12224 {ECO:0000313|EMBL:SDJ29834.1};
OS Rhodococcus triatomae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=300028 {ECO:0000313|EMBL:SDJ29834.1, ECO:0000313|Proteomes:UP000183263};
RN [1] {ECO:0000313|EMBL:SDJ29834.1, ECO:0000313|Proteomes:UP000183263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44892 {ECO:0000313|EMBL:SDJ29834.1,
RC ECO:0000313|Proteomes:UP000183263};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663}.
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DR EMBL; FNDN01000022; SDJ29834.1; -; Genomic_DNA.
DR RefSeq; WP_072740238.1; NZ_FNDN01000022.1.
DR AlphaFoldDB; A0A1G8SKY8; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000183263; 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 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; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817:SF76; PLASTIDIAL PYRUVATE KINASE 4, CHLOROPLASTIC; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 2.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDJ29834.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:SDJ29834.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183263};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDJ29834.1}.
FT DOMAIN 135..218
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 321..559
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
SQ SEQUENCE 599 AA; 64507 MW; C26F4AE3D289123B CRC64;
MTPDATGRRE RLEALRGALV QLRGDAAAAE RAATERIEHV DPAHRSAAAN LVRYRALRCH
DLRNLQVRLS QEGLSSLGRM ESDVLRNLDA VLGMLDAAIG DGRSSVPEPG PPDSEPWFEL
SANAAALLGG TPDDRTTRIM VTLPSDAASD ASLVRSFVHA GMNLARVNCA HDQHDAWSAM
ATHVRSAGEG VRIAMDLGGP KLRTGPIEAG PRVVKIKPSR DAAGRVVSPT TVWTGRAPLH
CGDPEVPITD SDWVERRVVG DRVTFREARG RTRTMAVVET TGTGVELVGD RTSYLVPGTI
LAVGEDATTV GALPATPQSL RVRRGDLLVL TSSLEPAVPT SDGRHRIGCT LPEAFGAVHE
GHRVLFDDGK IGGVVTSASE DEIHVSITSA PIRGTKLKAE KGINFPDTTL PIPALTDEDR
EDLDAVVALA DIVEISFVRT ADDVRELLGL LEEKDALDIG VVVKLETVAG FEALPEVLLE
LMRWKRVGVM IARGDLAVEA GFERLAEVQE ETLWLCEAAR VPVIWATQVL DSLADAGVPT
RAEVTDAAQG ERAECVMLNK GPYIVEAITA LDDILRRMHR HIYKKNPLLR KLGAWDVGE
//
