(data stored in SCRATCH zone)

SWISSPROT: A0KEE1_AERHH

ID   A0KEE1_AERHH            Unreviewed;       374 AA.
AC   A0KEE1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
DE            Short=N5-CAIR synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
DE            EC=6.3.4.18 {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
GN   Name=purK {ECO:0000256|HAMAP-Rule:MF_01928,
GN   ECO:0000256|RuleBase:RU361200, ECO:0000313|EMBL:ABK37904.1};
GN   OrderedLocusNames=AHA_0069 {ECO:0000313|EMBL:ABK37904.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM
OS   1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37904.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37904.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole
CC       ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR). {ECO:0000256|HAMAP-Rule:MF_01928}.
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole
CC       ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR). {ECO:0000256|RuleBase:RU361200}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP +
CC         hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole +
CC         ADP + 2 H(+) + phosphate; Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58730, ChEBI:CHEBI:137981, ChEBI:CHEBI:456216;
CC         EC=6.3.4.18; Evidence={ECO:0000256|HAMAP-Rule:MF_01928,
CC         ECO:0000256|RuleBase:RU361200};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01928,
CC       ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS01092012}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP-
CC       Rule:MF_01928, ECO:0000256|RuleBase:RU361200,
CC       ECO:0000256|SAAS:SAAS01092022}.
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DR   EMBL; CP000462; ABK37904.1; -; Genomic_DNA.
DR   RefSeq; WP_011704107.1; NC_008570.1.
DR   RefSeq; YP_854594.1; NC_008570.1.
DR   STRING; 380703.AHA_0069; -.
DR   EnsemblBacteria; ABK37904; ABK37904; AHA_0069.
DR   GeneID; 4488606; -.
DR   KEGG; aha:AHA_0069; -.
DR   PATRIC; fig|380703.7.peg.64; -.
DR   eggNOG; ENOG4105CY8; Bacteria.
DR   eggNOG; COG0026; LUCA.
DR   HOGENOM; HOG000034029; -.
DR   KO; K01589; -.
DR   OMA; ITFDHEH; -.
DR   BioCyc; AHYD380703:G1G7B-69-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01928; PurK; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF17769; PurK_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01161; purK; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KEE1.
DR   SWISS-2DPAGE; A0KEE1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|RuleBase:RU361200,
KW   ECO:0000256|SAAS:SAAS00098858};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
KW   Lyase {ECO:0000313|EMBL:ABK37904.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|RuleBase:RU361200,
KW   ECO:0000256|SAAS:SAAS00467005};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01928,
KW   ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00467012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   DOMAIN          108..290
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NP_BIND         148..154
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   NP_BIND         177..180
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   NP_BIND         260..261
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         104
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         143
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         185
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         208
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
SQ   SEQUENCE   374 AA;  39764 MW;  FBDA42203F38661E CRC64;
     MILPPATLGM LGGGQLGRYF VMAAHRLGYK VVVLDPDPAS IAGAAADHHI VAAYDDPTAL
     HDLASRCAAV TCEFENVPAT ALALLEQYQP VRPAAGAVRI CQDRREEKAF LSRAGIPVAP
     NQTLLPGEPL PALPASLFPA ILKTAREGYD GKGQWTIQAA DQLPAALAAS GVPCVLEQRL
     ALEGEFSLTL ARSPSGAIGA LPLVQNWHSG GILDQTRSPA NVPALEADAR RIAEQLIAAL
     DYVGVLTVEL FLVAGKLLVN ELAPRPHNSG HPSLDNAECS QFELQVRALC DLPLPSRIAV
     RPAMLLNLLG DLWQAGTPDW AALLALPGVH LHLYGKGEPR PGRKMGHVTI TAADWPTVEE
     TCQRVRQLLG LPPR
//

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