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Database: UniProt
Entry: A0A1E7L0Q0_9ACTN
LinkDB: A0A1E7L0Q0_9ACTN
Original site: A0A1E7L0Q0_9ACTN 
ID   A0A1E7L0Q0_9ACTN        Unreviewed;       438 AA.
AC   A0A1E7L0Q0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000256|HAMAP-Rule:MF_01928};
DE            Short=N5-CAIR synthase {ECO:0000256|HAMAP-Rule:MF_01928};
DE            EC=6.3.4.18 {ECO:0000256|HAMAP-Rule:MF_01928};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_01928};
GN   Name=purK {ECO:0000256|HAMAP-Rule:MF_01928};
GN   ORFNames=AN218_20660 {ECO:0000313|EMBL:OEV09750.1};
OS   Streptomyces nanshensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=518642 {ECO:0000313|EMBL:OEV09750.1, ECO:0000313|Proteomes:UP000176005};
RN   [1] {ECO:0000313|EMBL:OEV09750.1, ECO:0000313|Proteomes:UP000176005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 10429 {ECO:0000313|EMBL:OEV09750.1,
RC   ECO:0000313|Proteomes:UP000176005};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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   -!- 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   -!- 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}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01928}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP-
CC       Rule:MF_01928}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01928}.
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:OEV09750.1}.
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DR   EMBL; LJGW01000348; OEV09750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7L0Q0; -.
DR   PATRIC; fig|518642.10.peg.4589; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000176005; Unassembled WGS sequence.
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; 3.40.50.20; -; 1.
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   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   PANTHER; PTHR11609:SF5; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR   PANTHER; PTHR11609; PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF17769; PurK_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01928}; Ligase {ECO:0000256|HAMAP-Rule:MF_01928};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01928}.
FT   DOMAIN          137..352
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   BINDING         133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         236..239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         322..323
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
SQ   SEQUENCE   438 AA;  46936 MW;  2E6F9FF5C794F1BD CRC64;
     MRPWRRAARR RAGRPHTALR GRTPYGYAEV VTFPVVGMVG GGQLARMTHE AGIPLGIRFR
     LLSASAQESA ALAASDVVVG DHRDLATLRE FARGCDVITF DHEHVPTEHL RALEAEGVPV
     RPGPEALKHA QDKGVMRARL TQAGVPCPRH RVVRDPADVA AFAAELAAEL AAGPAADDGT
     SASADGDGSS PVSPVFPVPV VLKTVRGGYD GKGVWVVRTR DEAAVPFRAG VQVLAEEKVD
     FARELAACVV RSPHGQAVAY PVVESVQVGG VCDTVIAPAP GLDAERAVVA QELALRIAQE
     LGVVGHMAVE LFETRDGRVL VNELAMRPHN SGHWTQDGAV TSQFANHLRA VLDLPLGDPR
     ARARWTVMAN VLGGDYPDMY AAYRHCMARD PQLKIHMYGK DVKPGRKVGH VNTYGDDLAD
     VRERAAHAAG YLRGTISE
//
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