ID G3JBY5_CORMM Unreviewed; 1215 AA.
AC G3JBY5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Urea amidolyase, putative {ECO:0000313|EMBL:EGX93703.1};
GN ORFNames=CCM_01972 {ECO:0000313|EMBL:EGX93703.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX93703.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX93703.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX93703.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; JH126400; EGX93703.1; -; Genomic_DNA.
DR RefSeq; XP_006667189.1; XM_006667126.1.
DR AlphaFoldDB; G3JBY5; -.
DR STRING; 983644.G3JBY5; -.
DR GeneID; 18164001; -.
DR KEGG; cmt:CCM_01972; -.
DR VEuPathDB; FungiDB:CCM_01972; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_002162_0_1_1; -.
DR InParanoid; G3JBY5; -.
DR OMA; TLQMWNR; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000001610; 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: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; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR011761; ATP-grasp.
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 NCBIfam; TIGR00724; urea_amlyse_rel; 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; 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; 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; 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 Lyase {ECO:0000313|EMBL:EGX93703.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT DOMAIN 6..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 660..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 131819 MW; F20599206F433CCB CRC64;
MSAPTPSKRL LIANRGEIAN RILKTARLLN YCIISIYMPS DASSPHVTDS DVAVPVSSYS
DINEIVAIVR QQAVEFVIPG YGFLSENAQF AAAVEDAGAV FVGPAPEHIV MFGVKHTARD
VAAQVGVPIC PGSGIVQSAD EAVLEASRIG YPIMLKATAG GGGMGLKICK DESEVRSSFA
SVVSRGTALF SNPGVFLERY FPVSRHIEIQ VFGDGRGDCV AFGERECSIQ RRHQKVIEES
PSPFVAARPA LRQRLVQASR LLASSIRYRS AGTVEYLVDD ATGDFFFLEM NTRLQVEHGI
TELRFGIDLV ALMLQQAEQP LDLCDLKMLE PSGAAMEARI YAENPGKNYF PSPGQLQLVE
FSSDPGVRVD TWVQTGTNIS LAFDPLLAKV MVHAETRSCA VSKMRQALDK TKLRGVVTNT
DYVRRIFETE WFLQGQTTTT VLDSFQYTPR ALEIVAPGSY TTVQDFPGRV GVGFGIPEGG
PADALHARLA NCVAGNEPGC ELFEITFTGP TILFHGKAII ALAGGVVEAR LDGRPVSMYA
RIEVPAGSVV TIGRLLQGCR TYLAIQGGLP GIPTYLGSKS TSPIIEVGGH QGRPLVAGDL
LDIGAPAEFV PFTLPSALVP VLDLKTVYCL SGPHDSPDIM TSSGAEAIYA SEWTVSHQAS
RTGVRLDGPR PQWARQTGGQ GGSHPSNYLD YPYSLGALNW TGDSAVVFPA DAPSLGGFVT
SHVIPRAELC KIGQLKPGDQ FRFAQITLQS AMDLYQAQET YIQHVKRLAA GIKTSEALSS
LKLQAKSLAL STPSTAIIGT HGDVTIRQAG DSYVLVEFLQ SLQLEVRCKV QAVTEAIDNC
IIDGIHLVTP IGCSLLVQYD GFKICQAQLV DRIQSILGAH GASPLLSNKL SSRHIRLPMV
FDDKVNRASV ERYMKTQRPT ASYLPDPVEF IARSNGLESK HQVLEKVLST RILVVGVGFW
SGTPIGFPVD PRCRLMVPKF NPSRTFSPAG GLGIGGCFFC CDPTDAPGGY VNFGRTLPGW
DKFCVNKSFG KRPWLFENFD QLSFYVVDED EFERIYSRFQ AGKYQFDITP TEFDVVEYTK
FCESVADETT AFQARQKQAT EIETEKCGRL ARYQWLKEQT VERDAVPALE EIDDALKIDA
EMHASIYKIK IQKGDTLNNG DIMLILEAMK MEINIAVSAA QAGLVVDSVV VAPGDVVKPG
DVLVVLARPG EAKTG
//