ID A0A136NE58_9BACT Unreviewed; 490 AA.
AC A0A136NE58;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN Name=pyk {ECO:0000313|EMBL:KXK44429.1};
GN ORFNames=UZ05_CHB002002644 {ECO:0000313|EMBL:KXK44429.1};
OS Chlorobi bacterium OLB5.
OC Bacteria; Chlorobiota.
OX NCBI_TaxID=1617412 {ECO:0000313|EMBL:KXK44429.1, ECO:0000313|Proteomes:UP000070057};
RN [1] {ECO:0000313|EMBL:KXK44429.1, ECO:0000313|Proteomes:UP000070057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB5 {ECO:0000313|EMBL:KXK44429.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (OCT-2015) 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 -!- 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}.
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:KXK44429.1}.
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DR EMBL; LLZO01000311; KXK44429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136NE58; -.
DR PATRIC; fig|1617412.3.peg.2769; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000070057; 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 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; 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.
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:KXK44429.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 18..338
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 372..477
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 490 AA; 54730 MW; 4F217B17093ACA7C CRC64;
MSEQSRSNPE TEKKFSNKNT KILATLGPAA DTKEKIIELI QAGIDGVRLN FSHGGHEYYD
QVFKNVNDAC VATSEPIAIL VDLQGPKIRV GELLLPEYEL KENDHLEITM HDIVGTKEKF
SCSYEGLARD AKIGDHIYID DGLIKLLIIA IDHDSIFCVV LEGGTLKPRK GMNLPGMELS
LPSLSEKDFE DLDFALSHRV DFIALSFVRK ASDIYQLRNY LTEKGFEKNI IAKIEKPEAV
RNFDEILEAA DGIMIARGDL GVELPPQEVP VIQKSIIRKC NKAGKMVITA TQMLESMIHN
AVPTRAETSD VANAVWDGSD VVMLSGETSV GEYAVETVDM MQKILIETEA NMDLVKYERK
ETPKTSEDNV FDSVGKALAD MAVQLNAEAV VSFTRRGRMA RAMSRFRPNT KIIAMSDSFE
VMNVLRLIWG IIPVYFEDMP DEQVAIKAAK KILLDKKIVK EGDTVIFTSG APVDEKGKDI
WIRFAKARYY
//
