ID S5N940_9HEMI Unreviewed; 1810 AA.
AC S5N940;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Urea amidolyase {ECO:0000313|EMBL:AGR65722.1};
OS Planococcus citri (citrus mealybug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Coccoidea;
OC Pseudococcidae; Planococcus.
OX NCBI_TaxID=170843 {ECO:0000313|EMBL:AGR65722.1};
RN [1] {ECO:0000313|EMBL:AGR65722.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23791183; DOI=10.1016/j.cell.2013.05.040;
RA Husnik F., Nikoh N., Koga R., Ross L., Duncan R.P., Fujie M., Tanaka M.,
RA Satoh N., Bachtrog D., Wilson A.C., von Dohlen C.D., Fukatsu T.,
RA McCutcheon J.P.;
RT "Horizontal gene transfer from diverse bacteria to an insect genome enables
RT a tripartite nested mealybug symbiosis.";
RL Cell 153:1567-1578(2013).
RN [2] {ECO:0000313|EMBL:AGR65722.1}
RP NUCLEOTIDE SEQUENCE.
RA McCutcheon J.;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; KF021972; AGR65722.1; -; mRNA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 1.20.58.1700; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1.
DR InterPro; IPR014085; Allophanate_hydrolase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR02713; allophanate_hyd; 1.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000313|EMBL:AGR65722.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 602..1047
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 721..918
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1735..1810
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1810 AA; 197469 MW; 21AC66F4E96AC9AC CRC64;
MPKIGLTINE WNDHIGQNLN DAKNVLLDYL DKIMEKHEAW IYYATPEQII SQFDSLLPSL
RNSASNLPLF GVPFAVKDNI DVAGWPTTAA CPSFSYIAEA DATVVSRLKA AGAIVVGKTN
LDQFATGSVG TRSPFGIVKN SFNPQYISGG SSSGSAWVVA NGLVPFALGT DTAGSGRIPA
AFNNIVGLKP TKGWLSTKGV VPACCLNDTV SVFALTVEDA FTVATLAAAP DPDDCYSRTH
PATTPAAFQK IPVLAIPDKL KFFGDQLAEA AWLAALQKMN TLGVEIKTID FSPFYQLAEQ
LYGGAWIAER TAALGDILNH ATHMDPIVHS IVMEGTRFTA VEAWKAEYQR AQLVKHIQSI
LAEVDALLVP TSSTIRTIKE IQEEPIQYSS QLGIYASCTN LADLSALALP APFRADGLPA
GISLLALPWH DRALANFGQH WQKHLALPLG AISRSNQIKF NPLIPSLQHI QIAIPGNYSV
GTSSLHTLLR SNYAVLIKET TTAPHYNLHA VCDGFNKIPA LTHSNVGSTI AVELWEIPLG
LFGQFVAEIP PPLGLGSVTL SNGEVVKGII FCQLELPSDA VEITEAGSWS NWLASCKSSP
KKFTTVLIAN RGEIACRAIR TLKHLGIRSV AIYSDSDRNA LHVKNADVAI ALAGDKVNDT
YTNIEKILAA AKTSAAQAIW PGYGFLSESQ PFADACEKAG IVFIGPTPQQ IREFGLKHRA
RELATEAGLP ISPGTPLLNT IEEALEAAKK IGYPVMLKST AGGGGIGMTR CANESELQKA
WENVRHLSEQ FFGNADVFIE RCIDHARHIE VQIFGDGNGK VVALGERDCS LQRRNQKVIE
ETPAPNLPKA TRDLMLTASV QLGKLVKYRS AGTVEYIYDA STDVFYFLEV NTRLQVEHAV
TEYVTGIDLV ACMIQVAAGD SIDWSSLQKT PTGASIEVRL YAEDPIKNFQ PCPGLLTQVI
FPKGENVRID SGVETGSDVS PHYDPMIAKL IVYGETRDTA LQQLQDALSA TQLHGITTNL
DYLRQIVETD EFQSGNVWTG FLNNFTATSA AIEVLQPGTL STIQDYPGRI GYWDVGVPPS
GPMDDFAFRL ANRIVGNHES AAGLEFTLQG PTLKFREDAI ISLTGGYCAV ELDGNKVEYW
QPISIKTGQT LKVGRAQSGC RTYLAIRNGF DVPEYLGSRS TFTLGQFGGH AGRTLRVADV
LPISQPQLTV CTTPAPISSP QALDEVLIPI YGNIWTIKVL YGPHGAPDFL TQDSIDEFFA
TDWQVHYNSN RLGIRLIGPK PSWTRANGGE AGLHPSNIHD CMYAMGSVNF TGDFPVILTH
DGPSLGGFVC PVTIAKAELW KVGQVKPGDH IRFHPISVEE ALALEQAQTE TIETLLPVHM
PLYPSPSLAN TEFGSAAILA LIPGTATTPK AVYRQAGDNY ILIEYGEYSL DLALRLRVYL
LMNALHKCNV PGIAELSPGV ISLQVHYNSN ELSQSKLMTL LLDLEKTLGD VSRLKVPSRI
LWMPMAFEDS AALGAVQRYR ESVRATAPWL PNNVDFLQRI NGLPRREIVS DIIYAASWLV
LGLGDVYLGA SCAVPVDPRH RLLSSKYSPA RTFTAEGTVG VGGMYLSIYG MDSPGGYQLV
GRTLPIWNRF MQNPQFVDGK PWLLRFFDQI RFYPVSETEL TQLREDFRHG RTTIRIEETL
FDFVEYQHLL KDNASSIEKF RQFQAVAFEA EVALWAQEEQ NNPEPTGKDN SVPEVEEDEN
ALPVQADMNG NIWKVLVKSG DIVEASQTLV IVEAMKMELA INAPQKGRVK RIVCQPGHSV
SPGDTLLWLE
//
