KAD6_PYRAB
ID KAD6_PYRAB Reviewed; 180 AA.
AC Q9UZK4; G8ZKB5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00039};
DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00039};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00039};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00039};
GN OrderedLocusNames=PYRAB11420; ORFNames=PAB0757;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC catalyzes the reversible transfer of the terminal phosphate group
CC between nucleoside triphosphates and monophosphates.
CC {ECO:0000255|HAMAP-Rule:MF_00039}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00039};
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00039}.
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DR EMBL; AJ248286; CAB50053.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70558.1; -; Genomic_DNA.
DR PIR; H75093; H75093.
DR RefSeq; WP_010868259.1; NC_000868.1.
DR PDB; 4CVN; X-ray; 2.12 A; A/B/C/D=1-180.
DR PDB; 4CW7; X-ray; 2.46 A; A/C/E/G=1-180.
DR PDBsum; 4CVN; -.
DR PDBsum; 4CW7; -.
DR AlphaFoldDB; Q9UZK4; -.
DR SMR; Q9UZK4; -.
DR STRING; 272844.PAB0757; -.
DR EnsemblBacteria; CAB50053; CAB50053; PAB0757.
DR GeneID; 1496504; -.
DR KEGG; pab:PAB0757; -.
DR PATRIC; fig|272844.11.peg.1199; -.
DR eggNOG; arCOG01038; Archaea.
DR HOGENOM; CLU_079096_0_1_2; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 110798at2157; -.
DR PhylomeDB; Q9UZK4; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12595; PTHR12595; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..180
FT /note="Putative adenylate kinase"
FT /id="PRO_0000153910"
FT REGION 30..50
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT REGION 99..109
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:4CVN"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:4CVN"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4CVN"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:4CVN"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:4CVN"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4CVN"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:4CVN"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:4CVN"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4CVN"
SQ SEQUENCE 180 AA; 20205 MW; A6D0C05F18DB992A CRC64;
MLIAITGTPG VGKTTIAKLL AEKLGYEYVN LRDFALEKGC GREVDGEVEV EIDELAYFVE
KELKDRNVVL DGHLSHLMPV DLVVVLRAHP RIIGERLRER GYSKEKIGEN VEAELVDAIL
IEAIDEHENV IEVDTTNKTP EEIVEEIIGL IKSGVKRRVG IVDWSEVYDE IIPYLRLGGE
