ID E9FAL7_METRA Unreviewed; 1238 AA.
AC E9FAL7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 22-FEB-2023, entry version 64.
DE SubName: Full=Urea amidolyase {ECO:0000313|EMBL:EFY95203.1};
GN ORFNames=MAA_09279 {ECO:0000313|EMBL:EFY95203.1};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY95203.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFY95203.1, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:EFY95203.1, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFY95203.1}.
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DR EMBL; ADNJ02000003; EFY95203.1; -; Genomic_DNA.
DR RefSeq; XP_007825468.1; XM_007827277.1.
DR AlphaFoldDB; E9FAL7; -.
DR GeneID; 19263565; -.
DR KEGG; maj:MAA_09279; -.
DR HOGENOM; CLU_002162_0_3_1; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000002498; 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 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; 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 Lyase {ECO:0000313|EMBL:EFY95203.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 11..466
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 129..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1153..1235
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1238 AA; 133978 MW; D181674010D57C59 CRC64;
MGSIKVTSLR NIRKVLIANR GEIAVRCIKA CREVQVHSVA IFTHADATSL HVTLADEAVL
LPGDDGTAYT DGEAILDICK KTDADAVFPG YGFLSENAEF ARAVSSAGII FVGPSSASIK
AMGLKHEARA IAEAANVPVV PGTQLLSSAA EVVKAARDLG FPVMLKATGG GGGMGLQACD
TEIEVEKAFA TVQSRASTLF KNSGVFLEKY YPRSRHIEVQ VAGNGEIVIA FGERECSLQR
RHQKVIEECP SPFVERHSGL RERMLQAAIN YAARLKYKSV GTVEFLVDDE TADFFFLEMN
TRLQVEHGIT ELCYGVDLVH LMLLQADYER GGHVGIPSDI LRGLQRHSPR GSAIEARVYA
EVPLREFAPS PGILQLVHWP QGDGVRVDTW VRSGQRITPL YDPLIGKIMV HNPDGRGAAQ
SKMLAALRDT TLQGTQSNLE YLISIVASNI FINGRTLTNS LSMFKFKSCS LQVLDPGVMT
TIQDYPGRTA VGHGVPPGGP MDDLSARVAN SLVGNDWGVE LLEITLAGPE LLFHEAAVVA
ICGAELPVTV DGTPQPMWSR VIVSKDQILK LGKVSGSGTR TYLAVKGGFP QIPKFLGSKS
TAPELGFGGL QGRKLQAHDI LALAEESGIW AAAAAPLSLP AKAVPDFSIT SVGCLDGPFG
SDDILTPEGR KTLYEAQWAV SHNSGRSGVR LEGPRLKWAR TSGGGGGSHP SNVLDYGYPN
GGVNFTGESP IIFAHDRPDL GGFACPTTLC SAEMWKVGQL KAGNTIQLRS VSYDTALEIT
RKKEEYLGAI ILYAQGSACQ IPPLDVELSD EPPCSILHQT PPLGSHPRVT YRQGGDTSII
VEYGHQLPDL RNTACVQLLA NGLLAANLDG VRGDPNFATL TVRFDPLLTE RSKLLAHLIH
LDGQIGETTG IKIAARQVRL PVCLDHTSLR ESAQRYMENI RPSAAYMPDN VEYLRKNNAL
NDRRDVFDAI LKAPWLTVAV GFYVGTPVMF PLDPWRVLTG QKYNPSRVYT PGGSVGLGGS
LVAIYPVAAP GGYQLMGRTL GGWDSGGNRP GFSPEKPWLF NHFDLVTFYE VSEEEYNKME
QAFETGRYIF DITETTIDMD IYIARFDQAA KDPEYQAWRR RQVAASQEMG ELEQKLFEEW
TQAKSSGEGG SSFEDDGVDS GKVVLIESPV DANVWKVLVK QGDVLEKGQT VAVLEAMKME
INVVVSDDQA GAVVYTISQP PGSVVRPGAV VVRAVRPE
//