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Database: UniProt
Entry: A0A218VFD9_9PASE
LinkDB: A0A218VFD9_9PASE
Original site: A0A218VFD9_9PASE 
ID   A0A218VFD9_9PASE        Unreviewed;      1080 AA.
AC   A0A218VFD9;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Multifunctional protein ADE2 {ECO:0000313|EMBL:OWK64646.1};
GN   Name=AIRC {ECO:0000313|EMBL:OWK64646.1};
GN   ORFNames=RLOC_00005979 {ECO:0000313|EMBL:OWK64646.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK64646.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK64646.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK64646.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OWK64646.1}.
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DR   EMBL; MUZQ01000001; OWK64646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218VFD9; -.
DR   STRING; 299123.ENSLSDP00000011216; -.
DR   OrthoDB; 2898120at2759; -.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000197619; Unassembled WGS sequence.
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   Gene3D; 1.10.10.60; Homeodomain-like; 3.
DR   HAMAP; MF_02045; PurE_classII; 1.
DR   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR044822; Myb_DNA-bind_4.
DR   InterPro; IPR033626; PurE_classII.
DR   InterPro; IPR000031; PurE_dom.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   InterPro; IPR001005; SANT/Myb.
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; PF13837; Myb_DNA-bind_4; 3.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   SMART; SM01001; AIRC; 1.
DR   SMART; SM00717; SANT; 3.
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:UP000197619}.
FT   DOMAIN          5..69
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|SMART:SM00717"
FT   DOMAIN          195..259
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|SMART:SM00717"
FT   DOMAIN          460..512
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|SMART:SM00717"
FT   DOMAIN          921..1068
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   REGION          290..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1080 AA;  121196 MW;  ED6F591EDDFAA6A7 CRC64;
     MESGAGKHWT EEEVKALLSV WSEKNIRKQL HGTLRNKGIF IYIAKRLQEL GVCRDWKQCR
     AKYKNLKYEY RTVKYAHNSG DVTKTMKFFH DLDAILRYEP VTQLAAEENG RCSATEMQLN
     TSPTTDSTQG DVPVSLEDDE DVPGDPLLFI SHARPVQLGN KYLCLSPTPH NASNPASAVE
     ASKPAAFIPT VANEGGKHWT ANEVRALIRI WSDKNIQQQL EGTVRNKRIF EEVAARLQKF
     GIERDWKQCR TKYKNLKHEY KSVKSAQDSG STSKSMKFFN ELDAILGHCT TEQASKSDND
     ESERPPEWTE AKSEKDSVEM PGDTGEEDSV SNMSEDLQVA DTKKVSDSDD VTVNTTPENR
     AALHTTKETN MTKILEDESD LANSTPASLE ATQIKKETID IDDDSISTTS EDRSCTPVAK
     QMVGTENHIP LEEAQNHFKV ITINDTGAGK HWSDNEVRAL INIWSDEKIQ QMLEGATRNK
     EIFEEIARRL MKHGIDRDWK QCRTKYKNLK YEYRALQKEN EHLGNPKRKM RFYDEVDCIL
     RRQPLGTSGW GCESSSLLSV SVGDATANTG SLSTKRKTWN DEVSPVPLKK SASENAILHF
     QKLLTERVHT VTEGKKLLFE RLCKQEEMQD LNRKQLYTDP SVIQQVPAPA PAAAMAPAAS
     DLKLGKKVNE GKTKEVYELP DIPGCVLMQS KDQITAGNAA RKDRMEGKAA ISNTTTSCVF
     QLLQEAGIKT AFVRKQSDTA FIAAHCEMIP IEWVCRRIAT GSFLKRNPGV KEGYKFYPPK
     IEMFYKDDAN NDPQWSEEQI IEAKFCFAGL TIGQTEVDIM SRSTQAIFEI LEKAWQPQNC
     TLVDLKIEFG VNVLTKEIVL ADVIDNDSWR LWPAGDRSQQ KDKQSYRDLK EVTPEALQMV
     KRNFEWVSER VELLLKTKSQ GRVVVLMGSS SDLSHCEKIK KACATFGIPC ELRVTSAHKG
     PDETLRIKAE YEGDGIPTVF VAVAGRSNGL GPVMSGNTAY PVVNCPPLSA DWGTQDVWSS
     LRLPSGLSCP TTLSPEGAAQ FAAQIFGLNN HLVWAKLRSN MLNTWISLKQ ADKKLRECSL
//
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