ID R1GKI4_BOTPV Unreviewed; 489 AA.
AC R1GKI4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=UCRNP2_1021 {ECO:0000313|EMBL:EOD52200.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD52200.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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; KB915779; EOD52200.1; -; Genomic_DNA.
DR RefSeq; XP_007580342.1; XM_007580280.1.
DR AlphaFoldDB; R1GKI4; -.
DR STRING; 1287680.R1GKI4; -.
DR KEGG; npa:UCRNP2_1021; -.
DR eggNOG; KOG1212; Eukaryota.
DR HOGENOM; CLU_009600_9_2_1; -.
DR OMA; LPNCEEM; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000013521; 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; 2.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR46072:SF1; AMIDASE; 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 2.
DR PIRSF; PIRSF001221; Amidase_fungi; 2.
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:UP000013521}.
FT DOMAIN 77..240
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT DOMAIN 241..477
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 229
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 226..229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 489 AA; 52718 MW; 33C87E3A1CB69B44 CRC64;
MVDWRAVARD KRAAQAALIP PSLRLASVPD GLVDAVGHVE SCGLLSAEEL RLTATTDGRA
LASMLAAGEV SSAGVAAAFV KRAAALHQLT GCCTELFFDA ALRRAEALDR HLQETGEVVG
PLHGLPVSVK DGFDVEGVDS TVGWVGLVGK PAPRNGPEVE FLLGLGAVIY CKTNIPQSLM
MSDSYNHVFG QSVNPFNRNL ISGGSSGGEG ALVGGRGSIL GIGTDIGGSI RIPACLQGLY
DPWNVDPRLF PVPWRKELAE LPKKPLKLAF IFDDGVVKPQ PPVARAIREV AEKLKAAGHE
VVEWDTSLHE EGIKLWYKAV LADGGKKCRD TCALIGEPLI EGMVVGQEKD FLSIAQRQEL
SATKLAFEKT FLAQWNAAGI DGIIMPVLPW VNYTPKTWVR SKQWLGYSAL WNLLNYAALT
VPGSRVDAKV DQPGEEWKKH IPRNDSDAFN YEQYDVELVK GMPVGLQVVT GRFGEEKAVA
IAKVLESLK
//
