ID A0A1I2ENB1_9BACT Unreviewed; 621 AA.
AC A0A1I2ENB1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN ORFNames=SAMN05216283_102153 {ECO:0000313|EMBL:SFE93986.1};
OS Sunxiuqinia elliptica.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Sunxiuqinia.
OX NCBI_TaxID=655355 {ECO:0000313|EMBL:SFE93986.1, ECO:0000313|Proteomes:UP000198964};
RN [1] {ECO:0000313|EMBL:SFE93986.1, ECO:0000313|Proteomes:UP000198964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9156 {ECO:0000313|EMBL:SFE93986.1,
RC ECO:0000313|Proteomes:UP000198964};
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; FONW01000002; SFE93986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2ENB1; -.
DR STRING; 655355.SAMN05216283_102153; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000198964; 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 Gene3D; 2.40.33.10; PK beta-barrel domain-like; 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 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:SFE93986.1};
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:SFE93986.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198964};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFE93986.1}.
FT DOMAIN 130..217
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 360..573
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
SQ SEQUENCE 621 AA; 69957 MW; 4BCBBBD772B1091A CRC64;
MYQPQKLETI AQEISLILEK AIAMEKEYAQ ELRQVHPVYA KSAKNLIHYL AFRNFDVDHL
QNKLRELSLP SLSNIESHVV HSLLNIKTII NHLQGKQVVE KIPGVLTIPQ SKSLLTKNTK
MLLGSKSKNR RTRIMVTLPG IAAKHPQFIK RLLKLGMNSS RINCAHDNPE VWEKMIEQVK
NACPAKQRKC KIMMDLAGPK LRTGQMQPGP QVVHIKPKRN ALGRVTKPAQ VWLAPPGINP
PEGLVKAILP INEEYFEQLK KSDILSFEDT RGKKREIIID NKLDEGRIGL SYDSAFVETG
AVLTLQKEQK GNTINLKVGE LLPVEEAIIL HPGDPLILHK NPRNGEPASY SSRGKLVRPA
HISCTLPEVF KDVKVGNPIF FDDGKIEGII KKAHAEELHI EIIHAKTNGT RLRSDKGINL
PESDLKIRGL TNKDREDLRF VCKHADAVNL SFVNDQQDVQ DLLDVFQSLN QQVGIILKIE
TQKGFKNLPS ILLKAMQTYP IGVMIARGDL AIETGWKNFA SIQEEILRIC EAAHIPDIWA
TQVLESLAKK GVPTRSEITD AAMAQRAECV MLNKGAYIEK AVKMLDRILQ RMQHFNKKKE
TLLPRLNEAN QLQLSHDSYN S
//
