ID A0A369BLH5_9GAMM Unreviewed; 622 AA.
AC A0A369BLH5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN ORFNames=DFQ59_11843 {ECO:0000313|EMBL:RCX22430.1};
OS Thioalbus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalbus.
OX NCBI_TaxID=547122 {ECO:0000313|EMBL:RCX22430.1, ECO:0000313|Proteomes:UP000252707};
RN [1] {ECO:0000313|EMBL:RCX22430.1, ECO:0000313|Proteomes:UP000252707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26407 {ECO:0000313|EMBL:RCX22430.1,
RC ECO:0000313|Proteomes:UP000252707};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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:RCX22430.1}.
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DR EMBL; QPJY01000018; RCX22430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369BLH5; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000252707; 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, ECO:0000313|EMBL:RCX22430.1};
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:RCX22430.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252707};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RCX22430.1}.
FT DOMAIN 144..218
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 374..587
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
SQ SEQUENCE 622 AA; 66798 MW; 7ADC427D33228A4A CRC64;
MNLPAASIPD TDTTALADLL EQVRALRRQV LAAGQRRLET HHGHYPDGFS PSALNLAHYL
ALRAHDLRTL QDRLADAGLS SLGRCESHVL HSLDKVAGLL SLAVSCRPAE APEQPAPVNY
AQGRALLRAH AEALCGPRPA RGAYIMVTLP GEAARDPELT RALLARGMDC ARINCAHDGP
PEWTAMIANL RRAEAQTGRR CRVLMDLAGH KIRTGAIGPE PGAVHVKPRR DRLGRVTEPA
TVLLLRPGAA PPPGAGPWCF TPPEALFNRL GPGCRLHFTD TRGKSRTWEV TGAAAGAGWL
VRAPEGSYVG PGTRFRLDTG RDRRPGQAWP LSACTAGPAA MLLEAGDPLL LTRDTTPGHP
GRRDCSGVVV ESARIACTCP EALTGVRPGA HVWFDDGRLG TVVEASDAEG LRLRVTRAGP
RGVRLKPDRG INFPDTPLSL PALSAKDLRD LDFVAANADL VGFSFVQSLE DMERLLAELA
ARGAPRLPVV AKIETRLAVA NLPEILLGTL GRHPLGVMIA RGDLAVELGG ERMAEIQEEI
LWLCEAAHVP AIWATQVLES LAKKGVASRP ELTDAAMGVR AECVMLNKGP HILEALGTLD
DILTRMRAHQ RKKSARLRAL HW
//