ID H5XV45_9FIRM Unreviewed; 888 AA.
AC H5XV45;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Phosphoenolpyruvate synthase/pyruvate phosphate dikinase {ECO:0000313|EMBL:EHQ89643.1};
GN ORFNames=DesyoDRAFT_2577 {ECO:0000313|EMBL:EHQ89643.1};
OS Desulfosporosinus youngiae DSM 17734.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ89643.1, ECO:0000313|Proteomes:UP000005104};
RN [1] {ECO:0000313|EMBL:EHQ89643.1, ECO:0000313|Proteomes:UP000005104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ89643.1,
RC ECO:0000313|Proteomes:UP000005104};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M.,
RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA Woyke T.J.;
RT "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM
RT 17734.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; CM001441; EHQ89643.1; -; Genomic_DNA.
DR RefSeq; WP_007783491.1; NZ_CM001441.1.
DR AlphaFoldDB; H5XV45; -.
DR STRING; 768710.DesyoDRAFT_2577; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_9; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000005104; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EHQ89643.1};
KW Pyruvate {ECO:0000313|EMBL:EHQ89643.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005104};
KW Transferase {ECO:0000313|EMBL:EHQ89643.1}.
FT DOMAIN 21..332
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 811..882
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 888 AA; 98318 MW; 4DD975FE0BBEEA42 CRC64;
MTVSSATFFL TWDEAVQSGV QAAGGKGWNL GRLAQYGFKI PLGGILTTRA YEEFIKYNSL
QDTVNKITQS VTGENLDETN NQDKLKQLRQ KIKEGSLPPL IAEELKTKLD RMGILAKPLA
VRSSAAAEDS ARASFAGIHD SFLNVWGAEI FESVKGCYAS LWSNRAVAYR RKLQIRDEEV
MIGVVVLEMV EAQAAGVGFT CDPQTGRQDL VVINANFGLG EAIVAGTVEP DTYYLDASPW
NSVPHLVERK TGRKEGVTCL NQEGGTQFVQ TPESSGRQVL SEANIKKLGL LLLRVFEALG
GCDQHQDVEW VFDGRDFILV QSRPVTALPR STFAALKNQT DIWSNGNYRD ALPMVLSPLI
RRLTIATIDK ILKSNYTEIG YTLPEGLQFS RFFNGRLYCN LSALQWAMYD AMGALPRAFN
IGWGGHQPEI ELEDPKPYKG LRGLKRLWRG MRGVILINRA VKKAPETHAR VLNSFESLTE
KGFSHLQDKD LIQWYDELSK IAMEFTGKFS FLSGAASLPV GGLMKILSKY FGERAPMLLN
ALMVGGSAGI TSADHGYRLV ELAEIARRDN DAAQYFGSTA FDPIDWEGLP EHSAFKQEFR
EFIKEYGHRA VYELDIMNPR WNEDPSYLLN IIGSTIHTAD LSQFKAKQKE KFEQAWQEIE
RIVPANKHSS IKKLIRKAQE GAAVREKTKS VLAVMMEAYR KIAQELGSRF CRRAVIEEQA
DIYFCTWPEL VSLLNGEWDG AGLKVLIAGR KVFMKEMESI APPDIIMGDT PKYTEPVPRS
AGNFLTGVPV AAGKASGTAR LVRHPAEGNR LQPGDIMIAP STDPGWTPLF LKAGAVVMET
GGFLSHGAIV AREYGIPAVV NIPGVMGVIQ EGWKVDVDGD EGKVFLKD
//
