ID A0A1Z3HI49_9CYAN Unreviewed; 841 AA.
AC A0A1Z3HI49;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623, ECO:0000256|PIRNR:PIRNR000854};
DE Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996, ECO:0000256|PIRNR:PIRNR000854};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470, ECO:0000256|PIRNR:PIRNR000854};
GN Name=ppsA_1 {ECO:0000313|EMBL:ASC69960.1};
GN ORFNames=XM38_008900 {ECO:0000313|EMBL:ASC69960.1};
OS Halomicronema hongdechloris C2206.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nodosilineales; Nodosilineaceae;
OC Halomicronema.
OX NCBI_TaxID=1641165 {ECO:0000313|EMBL:ASC69960.1, ECO:0000313|Proteomes:UP000191901};
RN [1] {ECO:0000313|EMBL:ASC69960.1, ECO:0000313|Proteomes:UP000191901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2206 {ECO:0000313|EMBL:ASC69960.1,
RC ECO:0000313|Proteomes:UP000191901};
RX PubMed=26514405; DOI=10.1016/j.bbabio.2015.10.009;
RA Li Y., Lin Y., Garvey C.J., Birch D., Corkery R.W., Loughlin P.C.,
RA Scheer H., Willows R.D., Chen M.;
RT "Characterization of red-shifted phycobilisomes isolated from the
RT chlorophyll f-containing cyanobacterium Halomicronema hongdechloris.";
RL Biochim. Biophys. Acta 1857:107-114(2016).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988,
CC ECO:0000256|PIRNR:PIRNR000854}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001518,
CC ECO:0000256|PIRNR:PIRNR000854};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000854};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000854}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000854}.
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DR EMBL; CP021983; ASC69960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z3HI49; -.
DR KEGG; hhg:XM38_008900; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000191901; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01418; PEP_synth; 1.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 2.
DR PIRSF; PIRSF000854; PEP_synthase; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000854};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000854};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000854};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000854};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000854}; Pyruvate {ECO:0000313|EMBL:ASC69960.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000191901};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 35..138
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 147..391
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 432..503
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 525..837
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 841 AA; 92304 MW; 01582FB178D9C4DD CRC64;
MMVLSNRPQG SSSPARSKDT SFVLWFEEVG IGDIPLVGGK NASLGEMIQQ LSAKGVNVPT
GFATTAYAYR YFVENAGLED QLRNLFADLD LDDVTNLRER GKQARALVMN TPFPPELQAA
ISSAYLRLCE RYGADAEFCD RFSGEFADEC QKFGKELDVA VRSSATAEDL PDASFAGQQE
TYLNVHGVKA VLEACHKCFA SLFTDRAISY RHQYAERIDD FDEFSVALSV GVQKMVRSDL
AASGVMFSID TETGFKNAAL ITAAYGLGEN VVQGAVNPDE YFVFKPTLKD GKRPILNKRL
GSKEIKMVYD VGGGKQTKNV PVAVPDRKKF CISDDQVLTL AKWACIIEDH YSAKRGKDTP
MDIEWAKDGI TGDLFIVQAR PETVQSQKAG NVIKHYQLNG TGDVLTTGRA VGEMIGAGRA
RVIMDVHRIA EFQDGEVLVT NKTDPDWEPI MKKSSAIVTN QGGRTCHAAI IAREMGIPAI
VGCGDATEVL QTGQEVTVSC AEGEEGRVYG GRVPFDIQET QLDNLPRTRT RILMNVGNPE
EAFSLATIPC DGVGLARLEF IIANHIKAHP LALMHFDELE DKAAKWEISQ LTANYDNKPE
FFVDKLATGV GMIAAAFYPN PVVVRMSDFK SNEYANLLGG REFEPKEENP MIGWRGASRY
YDPNYTAAFG LECTAIKRVR DDMGMTNVIP MIPFCRTPDE GRKVLDTMAT YGLRKGENGL
QVYVMCEIPS NVILADQFSQ VFDGFSIGSN DLTQLTLGLD RDSALVAHIF DERNDGVKEM
VRQVITKAKG NDRKIGICGQ APSDYPEFAA FLVELGIDSI SLNPDTVLKT MLEIAKTEGI
G
//
