ID A0A1E3P043_WICAA Unreviewed; 520 AA.
AC A0A1E3P043;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=WICANDRAFT_95769 {ECO:0000313|EMBL:ODQ58237.1};
OS Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL
OS Y-366-8) (Yeast) (Hansenula anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=683960 {ECO:0000313|EMBL:ODQ58237.1, ECO:0000313|Proteomes:UP000094112};
RN [1] {ECO:0000313|EMBL:ODQ58237.1, ECO:0000313|Proteomes:UP000094112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8
RC {ECO:0000313|Proteomes:UP000094112};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001311};
CC -!- SIMILARITY: Belongs to the amidase family.
CC {ECO:0000256|ARBA:ARBA00009199}.
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DR EMBL; KV454212; ODQ58237.1; -; Genomic_DNA.
DR RefSeq; XP_019037444.1; XM_019186502.1.
DR AlphaFoldDB; A0A1E3P043; -.
DR STRING; 683960.A0A1E3P043; -.
DR GeneID; 30203748; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000094112; Unassembled WGS sequence.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR46072:SF11; AMIDASE-RELATED; 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR PIRSF; PIRSF001221; Amidase_fungi; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000094112}.
FT DOMAIN 73..502
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 117
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 217
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
SQ SEQUENCE 520 AA; 57602 MW; C35AA312248BFA6B CRC64;
MYKDNVEKKI KERDLQFPNE WLISSDRLPK DHDISQFIKS SNLLSDVEVE ITESTSSHIL
SSIKSQKWSA LQVITAFAHR ATIANQLVNP LSEELDQLLQ ETGKLKGKLH GLPISFKDEF
NIKGQYSTIG LVSFISNPPA SQDSPIVKIL RNEGAIFYVK TNVPIGAFNI VTFNNIFGKT
LNPFNRCLAS GGSSGGEAAL VAMKGSPLGI GSDLGGSVRQ PSSFQNLFAL KPSSLRFPHK
NTSIVSGLES LNGTNGPLST DIDSLKLYAQ VIVKSKPWLQ DFKVVPLEWK ELDLSSEKLR
FGVLIDDGVL RPTAPVKRAL DTVMAQLKKA GHEVVIWEAE DISEIAQFAN KFMTASGNKK
LVEAIEESGE PYPILQTMKD MPDIPTSTIW EWQEQRSNKV NEFLAKWNRL NLDGLISPVT
ALAGTDFENF VDVTYSPLPN VLDFPAGVFP VLRADANIDE PLDIKPRNET EKKVHSNYSP
EAINGGCVGL QVIGRKYEEE KVIEMVRLIS TTIGTIDYWK
//
