ID A0A1S2Y7W2_CICAR Unreviewed; 568 AA.
AC A0A1S2Y7W2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=amidophosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011941};
DE EC=2.4.2.14 {ECO:0000256|ARBA:ARBA00011941};
GN Name=LOC101506531 {ECO:0000313|RefSeq:XP_004500761.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004500761.1};
RN [1] {ECO:0000313|RefSeq:XP_004500761.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004500761.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58681; EC=2.4.2.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001546};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2. {ECO:0000256|ARBA:ARBA00005209}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138}.
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DR RefSeq; XP_004500761.1; XM_004500704.3.
DR AlphaFoldDB; A0A1S2Y7W2; -.
DR STRING; 3827.A0A1S2Y7W2; -.
DR PaxDb; 3827-XP_004500761-1; -.
DR GeneID; 101506531; -.
DR KEGG; cam:101506531; -.
DR eggNOG; KOG0572; Eukaryota.
DR OrthoDB; 4975at2759; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000087171; Chromosome Ca5.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR NCBIfam; TIGR01134; purF; 1.
DR PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11907:SF27; AMIDOPHOSPHORIBOSYLTRANSFERASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF13537; GATase_7; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 88..308
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 63..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 62096 MW; 8654249BF7AEC5A9 CRC64;
MAAPNLSSSL SLSLSNPKLF SSSSFSTFKP STISHPTFFH HKTLSFSTLK TNHKTLSSCN
NNNNNNTFPF TNTTSDQNDD DEKPREECGV VGIYGDPEAS RLCYLALHAL QHRGQEGAGI
VTVNNNNVLQ TVTGVGLVSE VFNDTKLRQL PGTLSIGHVR YSTAGQSMLK NVQPFVAGYR
FGSVGVAHNG NFVNYRKLRT ELEEKGSIFN TTSDTEVLLH LIATSKHRPF ILRIVDACEK
VQGAYSIVFV TEDKLVAVRD PFGFRPLVMG RRSNGAIVFA SETCALDLIE AKYEREVFPG
EVIVVDKNGV QSLCLMSHPQ PKQCIFEHIY FSLPNSVVFG KSVYESRRLF GEILATESPV
DCDVVIAVPD SGVVAALGYA AKAGVPFQQG LIRSHYVGRT FIEPSQKIRD FGVKLKLSPV
RAVLEGKRVV VVDDSIVRGT TSSKIVRLIK EAGAKEVHMR IACPPIIGSC YYGVDTPSSE
ELISNRMSVD EIKEFIGCDS LAFLPIDKLK NLLGDDSPNF CYACFSGVYP VEPTELKAKK
VGVELLEDGI NGLVQGKPNE KEVKIGGI
//
