ID A0A1U7ZQA8_NELNU Unreviewed; 430 AA.
AC A0A1U7ZQA8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=diaminohydroxyphosphoribosylaminopyrimidine deaminase {ECO:0000256|ARBA:ARBA00012766};
DE EC=3.5.4.26 {ECO:0000256|ARBA:ARBA00012766};
GN Name=LOC104595175 {ECO:0000313|RefSeq:XP_010254089.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010254089.1};
RN [1] {ECO:0000313|RefSeq:XP_010254089.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004882}.
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DR RefSeq; XP_010254089.1; XM_010255787.2.
DR AlphaFoldDB; A0A1U7ZQA8; -.
DR GeneID; 104595175; -.
DR KEGG; nnu:104595175; -.
DR eggNOG; KOG1018; Eukaryota.
DR OrthoDB; 5490680at2759; -.
DR UniPathway; UPA00275; UER00401.
DR Proteomes; UP000189703; Unplaced.
DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01284; Riboflavin_deaminase-reductase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR004794; Eubact_RibD.
DR NCBIfam; TIGR00326; eubact_ribD; 1.
DR PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11079:SF162; RIBOFLAVIN BIOSYNTHESIS PROTEIN PYRD, CHLOROPLASTIC; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 77..199
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 430 AA; 47518 MW; 8204B8C02E2AE9FF CRC64;
MHLQTLTQPT YILNSSSFLP YSCFIVPFQP VVPYPKCVYD SNFKNGFCSL FKRVPRLLTS
SRTHGGLIGI RCESFTDEDR FYMRRCVQLA KTAIGCTSPN PMVGCVIVKD GNIVGEGFHP
KAGQPHAEVF ALRSAGDSSE DATAYVSLEP CNHYGRTPPC TEALIRAKVK RVVVGMVDPN
PIVASKGVER LRESGIDVTV GVEEELCKNL NEAYIHRMLT GKPFTMLRYS LSVNGRILSQ
LGEGSTQSGG YYSQLLQEYD AVILSSTSFT EKSSFPTSQE PKANQPMKII VHRNPNLLMQ
IPTVPPEAAS QVIIFTAGDT ALNTELAQQG IETVVFDQIS LNTILDYCGC QGFCNVLLDI
QGDCDDLLEL IEDSLEQGLL QKVMMEVFPL WDGSEGSSFL ALKNLKRSFR LKKLKSTKVK
DSVLIEGYFC
//
