ID H2UTP8_TAKRU Unreviewed; 424 AA.
AC H2UTP8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=PurE domain-containing protein {ECO:0000259|SMART:SM01001};
GN Name=paics {ECO:0000313|Ensembl:ENSTRUP00000040322.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000040322.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000040322.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000040322.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004672}.
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 (carboxylase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004747}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC family. Class II subfamily. {ECO:0000256|ARBA:ARBA00010478}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase
CC family. {ECO:0000256|ARBA:ARBA00011020}.
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DR AlphaFoldDB; H2UTP8; -.
DR STRING; 31033.ENSTRUP00000081453; -.
DR Ensembl; ENSTRUT00000040464.3; ENSTRUP00000040322.3; ENSTRUG00000015780.3.
DR GeneTree; ENSGT00390000010172; -.
DR HOGENOM; CLU_061495_1_0_1; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000005226; Chromosome 20.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01416; SAICAR_synt_Ade5; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR HAMAP; MF_02045; PurE_classII; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR033626; PurE_classII.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR NCBIfam; TIGR01162; purE; 1.
DR PANTHER; PTHR43599:SF3; BIFUNCTIONAL PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE_PHOSPHORIBOSYLAMINOIMIDAZOLE SUCCINOCARBOXAMIDE SYNTHETASE; 1.
DR PANTHER; PTHR43599; MULTIFUNCTIONAL PROTEIN ADE2; 1.
DR Pfam; PF00731; AIRC; 1.
DR Pfam; PF01259; SAICAR_synt; 1.
DR SMART; SM01001; AIRC; 1.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000256|ARBA:ARBA00022793};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT DOMAIN 265..412
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
SQ SEQUENCE 424 AA; 46899 MW; DCA29BCAD0772870 CRC64;
DAAAKLKIGK KLNEGKTKQI FELLDQPGLV LVQSKDQITA GNAARKDQME GKAAIANKTT
SCVFKLLQES GIKTAFVKQH SDTAFIAAQC EMIPIEWVCR RVATGSFLKR NPGVKEGYRF
TPLKMEMFFK DDANNDPQWS EEQVLETKFS LAGLTIGQCE VDIMNRSTVA IFEILEKAWA
TQNCTLVDMK IEFGVNVKTQ EVVLADVIDN DSWRLWPSGD RSQQKDKQVY RDLKEVTPEA
MQMVKRNFEW VSERVELLLH SRASGRVVVL MGSTSDMAHC EKIRKACSSF GIPCVLRVTS
AHKGPDETLR IKAEYEGDGI PTVFVAVAGR SNGLGPVMSG NTAYPVINCP PLTPDWGAQD
VWSSLRMPSG LGCSTILSPE AAAQFAAQVF GLTDHQVWCK LRASMLNTWV SLKLADKKLQ
ACSL
//
