ID A0A0S8D0C5_9BACT Unreviewed; 438 AA.
AC A0A0S8D0C5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, 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};
GN ORFNames=AMK70_16225 {ECO:0000313|EMBL:KPK29266.1};
OS Nitrospira bacterium SG8_35_1.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704024 {ECO:0000313|EMBL:KPK29266.1, ECO:0000313|Proteomes:UP000052010};
RN [1] {ECO:0000313|EMBL:KPK29266.1, ECO:0000313|Proteomes:UP000052010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_35_1 {ECO:0000313|EMBL:KPK29266.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK29266.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJTK01000347; KPK29266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8D0C5; -.
DR PATRIC; fig|1704024.3.peg.3442; -.
DR Proteomes; UP000052010; 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}.
SQ SEQUENCE 438 AA; 48668 MW; F86DA1604FFE73E3 CRC64;
MLTSALNKRL PLIQEADLNG KIVLLRADHN VVKKGVIQDP FRIEQTIGTL YYIIDRGGRP
IIMSHVGRPK DKKTGRITCS PDESVQPVVE YLERKLNVQF HIPDCEIDPE LGISNLGKSI
YRAIGDLKNR KIGGIYLPNT RWFRGEEGEG FFRDNLAVLL ADLADIYVND AFGAWQPHVS
TYDVARFIPS YAGFLMQQEI ANLDKVIHLE PPFLAVIAGS KYDTKIGPLT AIYDKADHLI
LGGILYNAYL CAKYDISIQG IDNSDIKAAG DLVAKDRQHK KILEMPYIVE SEILGAKSEG
TYRTVAVSDF QKGDKYGYVL DIDPRSFEDP KVAEAIMKAK TVFVNAVMGL TPHFADGSRA
LYEELSKNTM SRKKFGGGDT LQEFKNLCPG LYLSVLDDPS YYFFTGGGTV LKAIEQGSPY
GLKPVIALME SKERLGGQ
//
