ID G7CH65_MYCT3 Unreviewed; 582 AA.
AC G7CH65;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Pyruvate phosphate dikinase {ECO:0000313|EMBL:EHI12175.1};
DE EC=2.7.9.1 {ECO:0000313|EMBL:EHI12175.1};
GN ORFNames=KEK_14788 {ECO:0000313|EMBL:EHI12175.1};
OS Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI12175.1, ECO:0000313|Proteomes:UP000004915};
RN [1] {ECO:0000313|EMBL:EHI12175.1, ECO:0000313|Proteomes:UP000004915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 /
RC 316 {ECO:0000313|Proteomes:UP000004915};
RG Tuberculosis Structural Genomics Consortium;
RA Ioerger T.R.;
RL Submitted (NOV-2011) 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:EHI12175.1}.
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DR EMBL; AGVE01000046; EHI12175.1; -; Genomic_DNA.
DR RefSeq; WP_003926439.1; NZ_AGVE01000046.1.
DR AlphaFoldDB; G7CH65; -.
DR PATRIC; fig|1078020.3.peg.2907; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR Proteomes; UP000004915; 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:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 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.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EHI12175.1};
KW Pyruvate {ECO:0000313|EMBL:EHI12175.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004915};
KW Transferase {ECO:0000313|EMBL:EHI12175.1}.
FT DOMAIN 23..272
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 398..469
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 582 AA; 61321 MW; 922F261F26ED9EB7 CRC64;
MTAQLTEPAV LRITDLETEP SRELVGGKAL SLWRMSRLGL RVPPAVVITT RSCAEYFSRG
RTLSDELFEE IVSGIGYLEE KTGRRLGASD KPLFVSVRSG AAVSMPGMMD TILNLGINET
TEAALAAESG NPQFAADVRR RFSALYGKLV AGCLEDLEDL PDTAAVLQAI SEETGSAVPD
DPYEALRGAV CAVFDSSQSR RAKAYRAHYG IPDDIGTAVT IQAMVFGNLD DDSGTGVVFT
RNPLTGSREP YGEYLPRGQG EDVVSGRVTP RPLSWLAENR PELHAELVSA AELLDREGRD
AQDIEFTVQH GTLYLLQSRA AKRTAQAAVR IATAMVEEGS IDPATACSRV TAEQVRHLLR
PAIDPDRIGD AEPIVTGTSA SPGYAVGIAV GTAEEAQAKP GSILVREATS PEDVHGMIAA
AAVVTEKGGS TSHAAVVSRA LDTPCVVGCG EGTSSALVGK LVTVDATGGR IYPGEIPGRA
TTVDDDEDLA TLLRWARDLA PIRVVPTADE VDGPVFDADQ ALIESGEELP TIPNGTHAVS
GAYFDTDEGV QAALDAGVSV IVSTNPLPVL LAAIAYRKDS DD
//
