ID K0NT33_DESTT Unreviewed; 993 AA.
AC K0NT33;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Predicted pyruvate phosphate dikinase, PEP/pyruvate-binding {ECO:0000313|EMBL:CCK82197.1};
GN OrderedLocusNames=TOL2_C40420 {ECO:0000313|EMBL:CCK82197.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK82197.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK82197.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
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DR EMBL; FO203503; CCK82197.1; -; Genomic_DNA.
DR RefSeq; WP_014959377.1; NC_018645.1.
DR AlphaFoldDB; K0NT33; -.
DR STRING; 651182.TOL2_C40420; -.
DR KEGG; dto:TOL2_C40420; -.
DR PATRIC; fig|651182.5.peg.4757; -.
DR HOGENOM; CLU_012339_0_0_7; -.
DR OrthoDB; 9812167at2; -.
DR Proteomes; UP000007347; 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; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCK82197.1};
KW Pyruvate {ECO:0000313|EMBL:CCK82197.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Transferase {ECO:0000313|EMBL:CCK82197.1}.
FT DOMAIN 436..811
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 993 AA; 112986 MW; 7B8DA4643233C8FE CRC64;
MNIENNKYIS EFHARSEVFR KLMAYEIKEI LLIASLYDMY NMEESGSLTS KIVNEYNGMN
LSHPPSVSGV SSVEEALSLL RQKEFDMVLI VPHLEELDLF SLGKKIKEIK KDLPVIIISP
SIREIYALPE NVLGECIDNI YIWSGNSDLF IALIKNAEDH LNVDQDTKLG NTRVLILVED
SPDYYSFFLP IIYKEIVTQT QALLKISLND NLKLLTMRAR PKVLLARNYE EAIELYEKYR
SFLLCVISDT RFPRNGETDP EAGIALLSKI KNENRNVPLL LISSESENRE KSDTIPAVFI
DKNSSTLSRD MHEFFQTHLG FGDFVFCLPD KQEIDRAENL LQLGAKLPKI PKESIAYHAD
RDHFSNWLMA RFEIDLALKF RAVKSSDFNC ADELRQFILS NINELRKKRQ KGIVSKFNRD
HFDPNIREFV KIGQGSLGGK GRGLAFVFGL LSKHEELQNN NSSINIKIPR TMVICTDIFD
DFVAMNNLQG FSKLGFTDDE VKEGFLNAQL PEWLIKDLEA YLAQVDYPLA VRSSNHLEDA
SFSPSAGLYK TYKLPNNHAS LSVRLDHMIA AIKLVYASVY SEDAKLFSLN GSNQPFTTSM
AVIVQEIAGD HYGDYFYPAI SGVAQSYNFY PFSRIKPEDG VAHFALGLGK TVVEGGKSLR
FSPKYPNIIP EFSSVENILQ NTQNSFYALK INNNLNAHQH LNLEKRTVND ANNEFPVQTL
ASTYVLGENR IRDTWDMPGP KVLTFARILK YNMPPISGLL TELLAFGSKS FGTPVEIEFS
VNLYPDQDRK TDFFFLQIRP MAIEENQFKI DITQQEIDHG FCFSSHALGN GINDKMTDIV
YVKPRDFKPE ATVQIAEEIN RLNSQLIQQK RSYLLVGPGR WGSSDRYLGI PVKWRNISGA
GAIIELRNES INADPSQGSH FFHNITPLGV HYITVDEIRK ESSTISNDYF DWEWIESLSA
ASETTFLRHI QLEKPLMMKI NGRNSQCVMT MKK
//
