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Database: UniProt
Entry: H6N3I4_GORPV
LinkDB: H6N3I4_GORPV
Original site: H6N3I4_GORPV 
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
//
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