ID A0A136KZI2_9CHLR Unreviewed; 259 AA.
AC A0A136KZI2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE Flags: Fragment;
GN Name=pgk_2 {ECO:0000313|EMBL:KXK14724.1};
GN ORFNames=UZ15_CFX003002990 {ECO:0000313|EMBL:KXK14724.1};
OS Chloroflexi bacterium OLB15.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1617416 {ECO:0000313|EMBL:KXK14724.1, ECO:0000313|Proteomes:UP000070332};
RN [1] {ECO:0000313|EMBL:KXK14724.1, ECO:0000313|Proteomes:UP000070332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB15 {ECO:0000313|EMBL:KXK14724.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000642,
CC ECO:0000256|RuleBase:RU000532};
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|RuleBase:RU000532}.
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:KXK14724.1}.
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DR EMBL; LMZS01000160; KXK14724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136KZI2; -.
DR STRING; 1617416.UZ15_CFX003002990; -.
DR PATRIC; fig|1617416.3.peg.3149; -.
DR Proteomes; UP000070332; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00162; PGK; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXK14724.1"
SQ SEQUENCE 259 AA; 26423 MW; 9265718FEC4D9F60 CRC64;
ALGDIYVNDA FGSAHRAHSS TAGVADYLPA VAGLLMEKEI NYLASAIENP TRPFAAILGG
AKVSDKIAVI DALLSKVDVL IIGGGMANTF LKAQGINVGA SLAEDDKLDT ARELLKKGGD
KLVLPVDVVL GDKFADDSDI LTVDVGSPIP DGWKIFDIGP KSVALFTEKL TPCKTVVWNG
PMGVFEKAPF AGGTNAIARV LAGLSVAGAT TIIGGGDSAA AVEQSGLADK ITHISTGGGA
SLEMLEGKTL PGVDVLQNL
//