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Database: UniProt
Entry: H9UKK8_SPIAZ
LinkDB: H9UKK8_SPIAZ
Original site: H9UKK8_SPIAZ 
ID   H9UKK8_SPIAZ            Unreviewed;       592 AA.
AC   H9UKK8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
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   OrderedLocusNames=Spiaf_2001 {ECO:0000313|EMBL:AFG38051.1};
OS   Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG38051.1, ECO:0000313|Proteomes:UP000007383};
RN   [1] {ECO:0000313|Proteomes:UP000007383}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC   {ECO:0000313|Proteomes:UP000007383};
RX   PubMed=23991249; DOI=10.4056/sigs.3607108;
RA   Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA   Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA   Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT   type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT   Rift.";
RL   Stand. Genomic Sci. 8:165-176(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   -!- 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}.
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DR   EMBL; CP003282; AFG38051.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9UKK8; -.
DR   STRING; 889378.Spiaf_2001; -.
DR   KEGG; sfc:Spiaf_2001; -.
DR   PATRIC; fig|889378.3.peg.1987; -.
DR   eggNOG; COG0469; Bacteria.
DR   HOGENOM; CLU_015439_0_2_12; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000007383; Chromosome.
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; 3.50.30.10; Phosphohistidine domain; 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:AFG38051.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007383};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          7..328
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          363..476
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   592 AA;  64138 MW;  01F212097141968C CRC64;
     MMMNTLRKTR IVCTIGPAVD DVETIKGMLK AGMNVARFNF SHDYHEIHAQ RIEKVRQASR
     ETKIPVAILL DTKGPEIRTG QIKDGGKINL ENGKKITLTT EQVEGTAELL SISYQKLPEE
     VTPGTHILVA DGVVDLEVES VDGNKIHCLI RAGGQLGSKK NVNVPGIKTS LPAITEKDRD
     DIVFGAKNNV DFIAASFIRK AADVQEILDL LAEHDSQTRV ISKIEDQEGL DNIDDIINVS
     HGIMIARGDL GVQLPPEKIP MAQKRITEKC NRQNKPVITA TQMLDSMINN PSPTRAELTD
     VANAIFDGTD AIMLSGETAS GDYPIKSVET MHNVAMAVET SPEFLERTEK YFAFHETTGE
     IGHAVAKSAY LLAQAVDATA IVTPTLRGNT PRLLSKFRPK QNVIAVTTSE TAYRQLLVQW
     GVFPILAEFV NNSEVMIQNA LRAAQKSGFI RRNDKVVTAA GLPLNSPIPM NTIKVHFMGN
     ILNRGQDGAG AKTAGLLIKG ETLSDAAAKA PKDTSYVLLA KTISSSDKLE LLKNAAGLIV
     EEPLTDLKAL TAINSDLVVV SGVPSAHAQF EEGLMVSLDG VEKIIYEGAL ED
//
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