ID W8L7Z3_9GAMM Unreviewed; 650 AA.
AC W8L7Z3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN ORFNames=M911_13295 {ECO:0000313|EMBL:AHK79965.1};
OS Ectothiorhodospira haloalkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=421628 {ECO:0000313|EMBL:AHK79965.1, ECO:0000313|Proteomes:UP000019442};
RN [1] {ECO:0000313|EMBL:AHK79965.1, ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|EMBL:AHK79965.1,
RC ECO:0000313|Proteomes:UP000019442};
RX PubMed=25057327; DOI=10.7150/jgen.9123;
RA Singh K.S., Kirksey J., Hoff W.D., Deole R.;
RT "Draft Genome Sequence of the Extremely Halophilic Phototrophic Purple
RT Sulfur Bacterium Halorhodospira halochloris.";
RL J Genomics 2:118-120(2014).
RN [2] {ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|Proteomes:UP000019442};
RA Singh K.S.;
RT "Draft Genome Sequence of extremely halophilic bacteria Halorhodospira
RT halochloris.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663}.
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DR EMBL; CP007268; AHK79965.1; -; Genomic_DNA.
DR AlphaFoldDB; W8L7Z3; -.
DR KEGG; hhc:M911_13295; -.
DR PATRIC; fig|1354791.3.peg.3149; -.
DR HOGENOM; CLU_015439_6_1_6; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000019442; 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; 2.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 2.
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; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817:SF76; PLASTIDIAL PYRUVATE KINASE 4, CHLOROPLASTIC; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AHK79965.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:AHK79965.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019442};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AHK79965.1}.
FT DOMAIN 402..612
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 70875 MW; C1402671F894C5E2 CRC64;
MQDSISEESH PSALDHPMDE TGPGQSATAT PPVDSLETLM AGLQNLRTEV LLGAHRRLER
FSRDYPGEVP LSARNLAHYL AFRSLDLRPI QRGLARQGLS SLGRTEAHVL ASINQVTRLL
GQLTGRPVAG LEDEPAIDYD TGATTLRDNA DQLFGPPSGP REVRIMVTLP SAAAVNPQLV
MELMEEGMDC ARINCAHDDA QAWSAMIGHL RAAEAQLGRR CTVLMDLGGH KLRTGPLEFK
PAITHIKPRR NLLGRVTEPA HVHLLPEGTG QDPVQARGQY AFSLPQATLD GLQSVDELRF
RDTRGKARVL RLVEPLPKGG WLATLDQGAY VSDETEFVLK RPDANGHLSP VLSLRLGWLT
REPVNIRLYK GALLHLTRDP VPGRPALVDD QGRLARCARI ACSAPEALDL LEVGQAVWID
DGKIGGRVES VDASGVMVRI THCRPQGSRL RADKGLNFPG ARLNLPPLSP QDMKDLDFVV
AHADLVGYSF VESRQDMVVL MDELARRGGA GLGVVAKIET GRALENLSEI ILATLGRHRL
GVMIARGDLA VEIGGERLAE IQEEILWLCE AAHVPVIWAT QVLETLARSG TISRPEITDA
AMAGRAECVM LNKGPYILEA VHTLNDILVR MQAHQHKKSS QLRALRLCAD
//
