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
//