ID A8UFH7_9FLAO Unreviewed; 479 AA.
AC A8UFH7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 76.
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 ORFNames=FBALC1_16482 {ECO:0000313|EMBL:EDP72716.1};
OS Flavobacteriales bacterium ALC-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP72716.1, ECO:0000313|Proteomes:UP000003630};
RN [1] {ECO:0000313|EMBL:EDP72716.1, ECO:0000313|Proteomes:UP000003630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALC-1 {ECO:0000313|EMBL:EDP72716.1,
RC ECO:0000313|Proteomes:UP000003630};
RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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:EDP72716.1}.
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DR EMBL; ABHI01000001; EDP72716.1; -; Genomic_DNA.
DR AlphaFoldDB; A8UFH7; -.
DR STRING; 391603.FBALC1_16482; -.
DR eggNOG; COG0469; Bacteria.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000003630; 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; IPR018209; Pyrv_Knase_AS.
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.
DR PROSITE; PS00110; PYRUVATE_KINASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003630};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 4..325
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 360..471
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 479 AA; 53164 MW; 5C2057D334EB82E1 CRC64;
MSNKKTKIVA TLGPATSSKT VLKAMLDEGA NVFRINFSHA DYKDVEERIK MIRELNEEFG
YNAAILGDLQ GPKLRVGTMK GEVIVSEGDE IIFATGKRFE GTKERVYMTY DNFPQDAKQG
ERILLDDGKL IFEVVSTDKK SEVKAKVIQG GPLKSKKGVN LPNTNISQPA LTEKDIEDAI
FAIGQKVDWI ALSFVRHAED LMQLEKLINE HSDHKIPIIA KIEKPEAVEN IDKIVAYCDG
LMVARGDLGV EIPAEEVPLI QKKLVLRAKK ARIPVIIATQ MMETMITSLT PTRAEVNDVA
NSVMDGADAV MLSGETSVGQ YPVQVIRQMA NIIRSVEDSP LIEVPQSPPH IRTKRYITKA
ICYHAANMAN EINAKAISTL TNSGYTAFQI SAWRPQAYIL VFTSNQRILT QLSLLWGVKA
FYYDKYVSTD ETIEDVNAIA CKKGYLDVGD MLISLAAMPI KDRGMVNTLR VTEIESCSF
//
