ID S7HUZ2_VIBFL Unreviewed; 487 AA.
AC S7HUZ2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=L910_3262 {ECO:0000313|EMBL:EPP19477.1};
OS Vibrio fluvialis PG41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1336752 {ECO:0000313|EMBL:EPP19477.1, ECO:0000313|Proteomes:UP000014854};
RN [1] {ECO:0000313|EMBL:EPP19477.1, ECO:0000313|Proteomes:UP000014854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG41 {ECO:0000313|EMBL:EPP19477.1,
RC ECO:0000313|Proteomes:UP000014854};
RX PubMed=23895343; DOI=10.1186/1757-4749-5-20;
RA Khatri I., Mahajan S., Dureja C., Subramanian S., Raychaudhuri S.;
RT "Evidence of a new metabolic capacity in an emerging diarrheal pathogen:
RT lessons from the draft genomes of Vibrio fluvialis strains PG41 and
RT I21563.";
RL Gut Pathog. 5:20-20(2013).
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:EPP19477.1}.
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DR EMBL; ASXS01000032; EPP19477.1; -; Genomic_DNA.
DR RefSeq; WP_020332453.1; NZ_ASXS01000032.1.
DR AlphaFoldDB; S7HUZ2; -.
DR PATRIC; fig|1336752.4.peg.4627; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000014854; 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; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF125; PYRUVATE KINASE II; 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:EPP19477.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 3..329
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 381..476
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 487 AA; 52226 MW; 6683334966C5B73E CRC64;
MCKTKIVATL GPASQSREKL TQLIQSGVNV VRLNFSHGSA EEHIARAELV RDIARTLNVS
VGVLVDLQGP KIRISCFETD VVQLTAGDTF ILDGQLGQQA GNQQRVGLDY PQLIADLTPG
NILLLDDGRI QLEVLDVNQA EQQVTTKVLN SGKLSNRKGI NLLGGGLSAP ALTDKDQQDI
ITAAKLNADF LAISFPRNGQ DIEYARKLAQ DAGCFAQIVA KVERAEVVSS LEAMDDMIQA
SDVIMVARGD LGVEIGDARL PSVQKALIAR TKHHGKPVIT ATQMMESMIE NPLPTRAEVL
DVANAILDGT DAVMLSAESA AGQYPVEAVQ AMVRIATGVE NEASCAQDCW DKLHHLCSDA
GKSFALSSMI SASKVHKDLG VAIITQKGET PLLMSRCQSQ ATIWAISDKP ELLNKLALLR
GVTPIYLPNI NPNADQLSQQ LLNVLRPEAE QKQISSILLT QLESVEGVGS VNVCRLLSLT
TPKDLAA
//
