ID H6N3I4_GORPV Unreviewed; 771 AA.
AC H6N3I4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Pyruvate phosphate dikinase, PEP/pyruvate binding domain-containing protein {ECO:0000313|EMBL:AFA72343.1};
GN OrderedLocusNames=GPOL_c12880 {ECO:0000313|EMBL:AFA72343.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA72343.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA72343.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
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DR EMBL; CP003119; AFA72343.1; -; Genomic_DNA.
DR AlphaFoldDB; H6N3I4; -.
DR STRING; 1112204.GPOL_c12880; -.
DR KEGG; gpo:GPOL_c12880; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_11; -.
DR OMA; EVPEMAY; -.
DR Proteomes; UP000009154; 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; 2.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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:AFA72343.1};
KW Pyruvate {ECO:0000313|EMBL:AFA72343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154};
KW Transferase {ECO:0000313|EMBL:AFA72343.1}.
FT DOMAIN 49..242
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT REGION 551..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 82935 MW; 00E1A0CB14AEE581 CRC64;
MTAATVEFDD ITDDRYGGKA AGLARLRALG LPVPVGFVVA DAPVDGSLDR VMARFGEMAA
AGTTPVAVRS SAAGEDGSEQ SFAGQYDTVL GVDFIDALTE AIHTCAASVH SARASAYSGH
TAATMNLVVQ RMVDSRAAGV VFTADPASGR RDLMVIDAVA GLGESLVDGT SAPDHLVLDE
EGAPVVAEYV AAPVLSPQEI DLIRAGGLRA AHEWGTPMDL EWAIDRSGDL WWLQARPITT
LPGDLNEMDS PVAGADHVYT RCNIGEMMPG AFCPLTASVS GFAIDYAMQT IQVVARAQEG
YYTPWLQVGY FYGHMFLNLT EGTALSSGIL GNSLEQFSTS ICGRVVDELQ PKPAQPFLRK
LGNTIRLTTH ALTVGPAIRR MPSDIAGFRV PAGSDPRAVL RQLDNGVELY CDITLTHVRS
SSRAAVAANV LESVMVRRAV DDGRDEDEGK AQAARLMAGA SRVESAEMLA ELDAVGQKIA
ADAAIADEFL SAAPEDAVTT LQAAPGDAGV ALRKFLERHS HRGYRELCMR DPSWADDPAG
LGTMMQVMVR SATERRGREP SRAPTPEHSS PTIRLLAHLA QGGARGREET KSRMALMAHQ
LKRGYRHLGE VLAESGRLPD ADLVFFFDRT ELRRVIDAED ITDLVQSAIR RREALSFQDS
LEFDDVSVGR PSPRLTVAER YIADDRIVGR PASRGVVEGT VRVAKTIGEA RDVRSGEILV
APVTDVGWTP YFTVVAALVT DFGLPRCRGR PRIRLTLRRE HPGRHSPAPD R
//