ID A0A1E4T9N7_9ASCO Unreviewed; 1806 AA.
AC A0A1E4T9N7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=Urea amidolyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CANCADRAFT_146769 {ECO:0000313|EMBL:ODV88470.1};
OS Tortispora caseinolytica NRRL Y-17796.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trigonopsidaceae; Tortispora.
OX NCBI_TaxID=767744 {ECO:0000313|EMBL:ODV88470.1, ECO:0000313|Proteomes:UP000095023};
RN [1] {ECO:0000313|Proteomes:UP000095023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17796 {ECO:0000313|Proteomes:UP000095023};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Jeffries T.W., Grigoriev I.V.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (FEB-2016) 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; KV453844; ODV88470.1; -; Genomic_DNA.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000095023; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000095023}.
FT DOMAIN 608..1050
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 727..924
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1730..1806
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1806 AA; 198397 MW; A645479CED354E11 CRC64;
MVQGWTISQW RDHMLGLKSS EGLSFLLDHL STLSSDDPAW IQIATPSLIT SQWENLQKLP
KAKDLPLYGV PCVVKDNIDV AGFNSTAACP AYSYLAAEDA VVVDHIKKAG AIVLGKSNLD
QFATGLVGTR SPYGKVPNAF SPNHVSGGSS SGSASTVARG IAPFSFGTDT AGSGRVPAGL
NNIIGLKPSL GLLSCTGVIP ACRSLDTVSI FALVLADAQL VFSIVAKYDP RDGFSRALPE
NPLTTFGPSP RFAIPDKPLW YNDTQNPELY EKALDNFKQI GVELVPNSFD ILYKLAACLY
EGPWVAERYA AISDFIKEHK EDMDPVVREI ILKAENFSAE DAFKYEYLRK NILRQVEIQF
ADVDGFIVPT CPLVPSFEDI AKEPIACNSK QGTYTNFVNL SDLSALAIPV GFRKDGLPFG
VTLISRKFND YALLDLAEKF LSPKERLLGN SNAVIAKNED RLIPGLPKPA PTVRVSVVGA
HLKGMPLHYQ LEDAKAVFVE KTSTSPNYKL YALAGTVPAK PGLRKVASGG VSIEIETYDI
PVENFGKFVS LIPGPLGIGS VELASGEIVK GFICEESGYS DPAAVDISHF GGWRKYIEST
KTASVKRPFD KVLIANRGEI AVRILKTLKK MKINSVSVYS ASDRYAPHAL EADEAIFLEG
DTAAETYLSI EKIIAAAKKT NAQAIIPGYG FLSENADFAE ACEKNSIVFV GPSASVINSM
GLKHSARAIA EKAKVPLVPG TGLLASLEET VAAAKKIEYP VMLKSTAGGG GIGLQRCNNE
EELVAAYDSV RRLGQQFFND SGVFLERFID NSRHVEVQIF GDGRGGAISL GERDCSLQRR
NQKVIEETPG PFIPEKVRMA LRQSAESLAR TMKYKCAGTV EFIYDSVREE FYFLEVNTRL
QVEHPVTEEV TGLDLVEWML LVAADTPPDF SQKIEIKGAS MEARLYAENP AKDFNPSPGQ
ITNVSFPDDA RIDTWISKGS EVSANYDPMI AKIIVYGKDR NEALDKLIKA LDETSVGGIV
TNIDYLRAIA RTSFFRSGDV YTRVLDTFSY KPNAVEVTAP GSYTTVQDYP GRKLLWHIGV
PPSGPMDDYA FRMANRLVGN HSNAPGIECT LMGPTFLFHR DGVAAVCGGE AKVTIDDEPV
SMWRPIQIRS GQKLSVGKLT SGCRSYIAIR GGIDVPEYLG SRSTFALGNM GGFNGRILKF
GDVIFLGDES VKACEIPAPV SEPVEPSTAV IPRYPKTWKI GVMAGPHTSP DFFLPQSIET
FLSSEWKVHY NSNRFGVRLI GPKPEWARKD GGEAGLHPSN AHDYVYAIGA LNFTGDEPVI
LTCDGPSLGG FVCPVTVVEA EMWKVGQLKP GDMIQFVLVD FQGALQLKKA YDDVIENLKD
AVPENLVLSI QSKLEDPVLY RSEAKDGIPK IVYRQAGDRY ILVEYGDNVL DLRMPYRVYR
LTQLVFKNYT TGVIEMSPGV RSVLIEFNGA KTSQKKLLDT LIKYENELVF DDNWTVPCRR
IRLPMAFEDS KTLAAVQRYQ ETIRSKAPWL PNNVDFLQKV NQLDSRDKIK DLMYRAQFLV
LGVGDVFLGA PCAVPLDPRD RLVGTKYNPS RTFTPEGTVG LGGMYMCIYG MDSPGGYQLI
GRTIPIWDKL VLGQQDRPWL VDPFDIIEYY PISEEELDKL SEEVKHGRYT IDITQSVFNH
GEYCKWMEEN KTSIDEYQKH VMEGTEEIAK LIQVANDELE QSSMSNAIED EDFGEDAVMV
YGEVAGRFWK GLVQPGDKVV KGQGLIVVEA MKTEMTVTAP QDGEVLKVCH KSGDFVEAGD
LVAVLK
//
