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Database: UniProt
Entry: D1PFW7_9BACT
LinkDB: D1PFW7_9BACT
Original site: D1PFW7_9BACT 
ID   D1PFW7_9BACT            Unreviewed;      1034 AA.
AC   D1PFW7;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Pyruvate phosphate dikinase, PEP/pyruvate binding domain protein {ECO:0000313|EMBL:EFB34406.1};
GN   ORFNames=PREVCOP_06125 {ECO:0000313|EMBL:EFB34406.1};
OS   Segatella copri DSM 18205.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=537011 {ECO:0000313|EMBL:EFB34406.1, ECO:0000313|Proteomes:UP000004477};
RN   [1] {ECO:0000313|EMBL:EFB34406.1, ECO:0000313|Proteomes:UP000004477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18205 {ECO:0000313|EMBL:EFB34406.1,
RC   ECO:0000313|Proteomes:UP000004477};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFB34406.1}.
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DR   EMBL; ACBX02000037; EFB34406.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1PFW7; -.
DR   STRING; 537011.PREVCOP_06125; -.
DR   PaxDb; 537011-PREVCOP_06125; -.
DR   HOGENOM; CLU_012339_0_0_10; -.
DR   Proteomes; UP000004477; Unassembled WGS sequence.
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   InterPro; IPR013815; ATP_grasp_subdomain_1.
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.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EFB34406.1};
KW   Pyruvate {ECO:0000313|EMBL:EFB34406.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004477};
KW   Transferase {ECO:0000313|EMBL:EFB34406.1}.
FT   DOMAIN          481..856
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
SQ   SEQUENCE   1034 AA;  118342 MW;  67117B2D2423E94F CRC64;
     MLKDASKSQK ISIFAQTLTS FMENNIPQEW NKFYLKDVSF VNLMMRRIYN VLIVANPYDA
     FMLEDDGRIE EKIYNEYMEL GLRYPPTFTQ VSTTEEAAAV LRSTVIDLVI CMPGNADNDA
     FDVARDIKGK FPNIHCVVLT PFSHGITKRM QNEDLSIFDY VFCWLGNTNL ILSIIKLIED
     KMNLEHDIQE AGVQMILLVE DSIRFYSSIL PNLYNYILEQ SKNFSQEALN RHAATMRMRG
     RPKVVLARTY EEAQKLYDKY SDNTLGVISD ARFPLKSAAK AFGNEVMPEV KPKHRTDTFG
     REKCPDAGLQ LFRYIRKNDP FVPLIIESSE SENRAKAEAE GFRFVDKNSK KMSVDLRRLM
     EEHMGFGDFI FRDPETHEEI MRIHSLKELQ DNIFNIPNDS MLYHISRNHM SRWLCARAIF
     PVSAFLKHVT WEKLQDVDAH RQIIFDAIVQ YRHMKNIGVV AVFDRMKFDK YAHFARIGEG
     SLGGKGRGLA FLDNIIKRHP EFNQYENATV QIPKTVVLCT DIFDEFMMSN NLYPIALSDA
     SDDEILKHFL HAQLPDSLIA DFFTFFEATR SPIAIRSSSL LEDAHYQPFA GIYSTYMIPY
     LEDKYQMLQM LACAIKGVYA SVFYRDSKAY MTATSNVIDQ EKMAVILQQV VGKDYGTRFY
     PTMSGVLRSL NYYPIGDEEA EEGIASLALG LGKYIVDGGQ TLRVCPYHPN QVLQTSETEL
     ALRDTQTQFY ALDMKHVGND FKVDDGFNIL KLRVKDAVED QSLTYIASTF DPYDQVINDG
     VYENGRKLIT FSSVLQHGVM PLPEILQMSM KYGAGAMRRP VEIEFACNIN NDRTCEFYLL
     QIRPIVDAKE MLDEDVKAIP DSDCLLRSHN SLGHGISEDV VDVVYVKYDD HFSAMNNFYV
     ADDIERINRK FLADGKNYVL IGPGRWGSSD HYLGVPVKWP HISAARVIVE VALKNYNIDP
     SQGTHFFQNL TSFGVGYFTV DTNTGEGGFV NKEILDAMPA VEETQYVRHV RFEHPMRILM
     DGKKQEGAVL IPKE
//
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