ID Q2NH60_METST Unreviewed; 306 AA.
AC Q2NH60;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=2-phosphoglycerate kinase {ECO:0000256|HAMAP-Rule:MF_00769};
DE Short=2PGK {ECO:0000256|HAMAP-Rule:MF_00769};
DE EC=2.7.2.16 {ECO:0000256|HAMAP-Rule:MF_00769};
GN Name=pgk2-1 {ECO:0000313|EMBL:ABC56843.1};
GN Synonyms=pgk2 {ECO:0000256|HAMAP-Rule:MF_00769};
GN OrderedLocusNames=Msp_0443 {ECO:0000313|EMBL:ABC56843.1};
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860 {ECO:0000313|EMBL:ABC56843.1, ECO:0000313|Proteomes:UP000001931};
RN [1] {ECO:0000313|EMBL:ABC56843.1, ECO:0000313|Proteomes:UP000001931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3
RC {ECO:0000313|Proteomes:UP000001931};
RX PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
CC -!- FUNCTION: Catalyzes the phosphorylation of 2-phosphoglycerate to 2,3-
CC diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3-
CC bisphosphoglycerate, a thermoprotectant. {ECO:0000256|HAMAP-
CC Rule:MF_00769}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate + ATP = (2R)-2,3-bisphosphoglycerate +
CC ADP + H(+); Xref=Rhea:RHEA:42408, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58248, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:456216; EC=2.7.2.16; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00769};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00769};
CC -!- PATHWAY: Thermoadapter biosynthesis; cyclic 2,3-diphosphoglycerate
CC biosynthesis; cyclic 2,3-diphosphoglycerate from 2-phospho-D-glycerate:
CC step 1/2. {ECO:0000256|HAMAP-Rule:MF_00769}.
CC -!- SIMILARITY: Belongs to the 2-phosphoglycerate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00769}.
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DR EMBL; CP000102; ABC56843.1; -; Genomic_DNA.
DR RefSeq; WP_011406043.1; NC_007681.1.
DR AlphaFoldDB; Q2NH60; -.
DR STRING; 339860.Msp_0443; -.
DR GeneID; 41325017; -.
DR KEGG; mst:Msp_0443; -.
DR eggNOG; arCOG01967; Archaea.
DR HOGENOM; CLU_848909_0_0_2; -.
DR OrthoDB; 358692at2157; -.
DR UniPathway; UPA00551; UER00609.
DR Proteomes; UP000001931; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00769; 2PGK; 1.
DR InterPro; IPR020872; 2PKG.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR33477; P-LOOP NTPASE DOMAIN-CONTAINING PROTEIN LPA1 HOMOLOG 1; 1.
DR PANTHER; PTHR33477:SF3; P-LOOP NTPASE DOMAIN-CONTAINING PROTEIN LPA1 HOMOLOG 2; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00769};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00769, ECO:0000313|EMBL:ABC56843.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00769}; Reference proteome {ECO:0000313|Proteomes:UP000001931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00769}.
FT DOMAIN 1..90
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 306 AA; 34706 MW; 32D644E4137DAAAE CRC64;
MLLIEGEIGG KKYREPFSKG ILSKSLVRCE IKADRAYELA SEIEKSFEKD KITIVPSEEL
IKRVKATLEK EDPLLAKKYS AWKNIRRSED PLIILIGGAS GIGTSSISFE LANKLGIKNM
LSTDMIREVM RKIVSKELCP TLFESSYTAA ESLTTPAPPE FDKTLLGFKD HVNTVSVGLT
GVVERSIKEG ISIVIEGVHI VPGFIDEELL NTPNVHMFVL SLSDEEIHKS RFYSRCRQLW
ARRPLKRYLK HFTDIRKTHD YIVGEANKYG IPVIENIDVT ATIDTMIEHI IDEKQLEKEV
KKQNEE
//
