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Database: UniProt
Entry: A0A370X2K5_9GAMM
LinkDB: A0A370X2K5_9GAMM
Original site: A0A370X2K5_9GAMM 
ID   A0A370X2K5_9GAMM        Unreviewed;       490 AA.
AC   A0A370X2K5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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:RDS82643.1};
GN   ORFNames=DWU99_14730 {ECO:0000313|EMBL:RDS82643.1};
OS   Dyella psychrodurans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1927960 {ECO:0000313|EMBL:RDS82643.1, ECO:0000313|Proteomes:UP000255334};
RN   [1] {ECO:0000313|EMBL:RDS82643.1, ECO:0000313|Proteomes:UP000255334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4MSK11 {ECO:0000313|EMBL:RDS82643.1,
RC   ECO:0000313|Proteomes:UP000255334};
RA   Gao Z., Qiu L.;
RT   "Dyella monticola sp. nov. and Dyella psychrodurans sp. nov. isolated from
RT   monsoon evergreen broad-leaved forest soil of Dinghu Mountain, China.";
RL   Submitted (JUL-2018) 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   -!- 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:RDS82643.1}.
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DR   EMBL; QRBF01000005; RDS82643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370X2K5; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000255334; 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; 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.
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, ECO:0000313|EMBL:RDS82643.1};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:RDS82643.1}.
FT   DOMAIN          8..330
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          362..475
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   490 AA;  52004 MW;  760C52CA67936900 CRC64;
     MTTDTHSRRT KIVATLGPAT DAPGMLERII SEGVNVVRLN LSHGQSDDHR ARAVAVRKAA
     EKVGCEVGIL ADLQGPKIRV ERFANGPVEL RDGDPFVLDC RADAPAGDAT RVGVSYLGLP
     NDVKAGDVLL LDDGLVALTV LEVVGTEIRC KVLIGGRLSD RKGLNRQGGG LSVSALSDKD
     KADIKLAAEI GADFLAVSFV RSGADMELAR QLLHEAGGKA SLVAKIERAD AIPVLGEIID
     ASDVVMVARG DLGVEIGDAE LPGLQKKIIR ETVQRNRAVI TATQMLQSMV RSPIPTRAEV
     LDVANAVIDG TDAVMLSEES AAGAHPDKAV AALRRICLGA ERQFEPKEDL ATAGHRLDRT
     DQAIALASML LASEIGVRAI VALTESGATA QWLSRYRSAV PIYALSPFDD ARRRMLVLRD
     VQPVKFTHDT LNPAVSAREA VRQLFTMGKL AEGDRVVLTH GDHIGRGGGT NTLKLLSVGA
     DGVVESLRDL
//
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