(data stored in ACNUC7421 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   08-MAY-2019, entry version 87.
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 /
OS   JCM 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.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-
CC       aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-
CC       carboxyaminoimidazole ribonucleotide (N5-CAIR).
CC       {ECO:0000256|HAMAP-Rule:MF_01928}.
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-
CC       aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-
CC       carboxyaminoimidazole ribonucleotide (N5-CAIR).
CC       {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-
CC         ribosyl)imidazole + ADP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58730,
CC         ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.4.18;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01928,
CC         ECO:0000256|RuleBase:RU361200};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC       amino-1-(5-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; APRTHNS; -.
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   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01928,
KW   ECO:0000256|RuleBase:RU361200}; Lyase {ECO:0000313|EMBL:ABK37904.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01928,
KW   ECO:0000256|PROSITE-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       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   NP_BIND     148    154       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   NP_BIND     177    180       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   NP_BIND     260    261       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   BINDING     104    104       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   BINDING     143    143       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   BINDING     185    185       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   BINDING     208    208       ATP. {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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