ID A4C5V0_9GAMM Unreviewed; 897 AA.
AC A4C5V0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Phosphoenolpyruvate-utilizing enzyme {ECO:0000313|EMBL:EAR29354.1};
GN ORFNames=PTD2_11079 {ECO:0000313|EMBL:EAR29354.1};
OS Pseudoalteromonas tunicata D2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR29354.1, ECO:0000313|Proteomes:UP000006201};
RN [1] {ECO:0000313|EMBL:EAR29354.1, ECO:0000313|Proteomes:UP000006201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2 {ECO:0000313|EMBL:EAR29354.1,
RC ECO:0000313|Proteomes:UP000006201};
RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR29354.1}.
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DR EMBL; AAOH01000002; EAR29354.1; -; Genomic_DNA.
DR RefSeq; WP_009837228.1; NZ_AAOH01000002.1.
DR AlphaFoldDB; A4C5V0; -.
DR STRING; 87626.PTD2_11079; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_6; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000006201; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
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 Pyruvate {ECO:0000313|EMBL:EAR29354.1}.
FT DOMAIN 27..314
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 817..889
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 897 AA; 100595 MW; 7DDA58D27F7B2DC0 CRC64;
MINAAMKLST ESDNIFRFTD MPLQSVSHIG GKGASLCAMS AAGLPVPAGV CLSVALFDDF
AAHIELLTRF DLTEGYEQWQ AAAKAIKESP LPNTLQDTIS AAIAHLKGPL AVRSSALDED
GESSSFAGQH LTKLALCGLD TILDAIKECW ASAFSEAAYR YRQHTDKHLD MPRMAVVVQQ
MQFGDVSGVA FGQHPTTFAR DAFLVENCFG LCEGLVSGQV VSDSWQIDKA SGEVREVTIA
DKSEQIIYLD GEIQKVAVSD EQRQQPALGP MAQQALYTLL CKVEAYFGVP QDVEWTWSEG
KIWLLQSRPI TTHAPQLDDF YLGSRDVDLQ KTMLWSRMDI GEIFTGRMTP LGLSFARYYQ
QQVHTGCGKG LGLLDLGEAD ETIAYYRGHV YLNVSYTAWQ LAQTPIGEDQ LPFLQRFSSE
AIDLAGYRNP YGEKHSHQDY SAKQCTRYWL KKNIKELFCA KRRARSMIAS RYKQFDRAQQ
KPLQQLSLEQ LAAEMRHALA YFKAMHEGYL PYYINAFACY GILEELSALW LGDKGKQLHN
QIKGDMSNLR TVASAQELWL LCQQLADWPQ VKQAFLDLEL DELEVFLNEH QAGIKYSRGP
LAQFMRENGV RAREEMELTH PRWLDDRTYL LQMIKVYLHQ GYAVDDAIAT QQRKQRKNSN
EILKTIPWYQ RRVMKLVISL YSGCAKLREE TRMSMVTSIW LVRRIVYELG QRLVATQQLT
SLDDIAYLDF AEILSYLEKR IDVHQLTEPA KLAQRQSAYH LWQSMPEPPL TFIGSPKSQP
DLILDPTLTQ LSGLATSAGF CRGKACVITD LAKQAGQFKK GDILIAPFTD ASWTPLFALA
GAVVTDIGSM LSHSSIVARE FGIPCVVNTN HASALFKSGD MLIVDAQNGI VVLDKES
//
