ID A0A2A4G9Q8_9FLAO Unreviewed; 601 AA.
AC A0A2A4G9Q8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN ORFNames=B7P33_05925 {ECO:0000313|EMBL:PCE64708.1};
OS Sediminicola luteus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sediminicola.
OX NCBI_TaxID=319238 {ECO:0000313|EMBL:PCE64708.1, ECO:0000313|Proteomes:UP000219559};
RN [1] {ECO:0000313|EMBL:PCE64708.1, ECO:0000313|Proteomes:UP000219559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HQA918 {ECO:0000313|EMBL:PCE64708.1,
RC ECO:0000313|Proteomes:UP000219559};
RA Chen L.;
RT "A new member of the family Flavobacteriaceae isolated from ascidians.";
RL Submitted (APR-2017) 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}.
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:PCE64708.1}.
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DR EMBL; NBWU01000002; PCE64708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4G9Q8; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000219559; 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; 2.
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 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};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000219559};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 128..218
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 346..560
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT REGION 582..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 67586 MW; A43E992AD98E0010 CRC64;
MKTKQLKKLH AQLETLIFFL EESQRAYRKK IKKTHPSHTE STKNLVHYLA LRKIDLAKTQ
GKLEILGLSR LARSESYVLD GLRKSREHVS ALLEKEKVNL NFEIPSAKNR LKLHHNTTDL
LGDIDSKRRV GIMVTMPSES VTNPKIISAF MQQGMDVARV NCAHDTSAEW KAIIDQIKSL
EDKFDKKVTI SMDLAGPKVR TGAMTPGPAV RKIKPMRDVY GNIKIPATVR LTEAPMAHND
IPVPTKWIKK LQIGDTVKLW DARGKKRRFI VTEYHGDHAV IQGMQTTYFE TGLRLQSHGQ
VTQILNLPNL ETAIHLQSGD LLVLHKEQIW GKTARLHESG QPIPAQISCT SPVPFKHVRI
QDRVFFDDGK IEGRVIRASS KKMIIKIETT KIGGVKLKTD KGINFPDTDL PLVGLTKKDR
QDLDFITDHA HVINFSFVNS AQDVKELQQI LREKGVLQNI GVVLKIETKT AFNNLGDILL
EAMKMKKVGI MIARGDLAIE VGWDKIGWVQ QEILSICAAA HVPVIWATQV FENYAKNGLP
SRSEISDVTM ALKAECVMLN KGPHISGAIK LLDQMLGGME KYQSKSHKMM PSLKKLPKSN
R
//
