ID A0A109FN27_9BASI Unreviewed; 1262 AA.
AC A0A109FN27;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=RHOSPDRAFT_24096 {ECO:0000313|EMBL:KWU46949.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU46949.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU46949.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU46949.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ954465; KWU46949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FN27; -.
DR STRING; 1305733.A0A109FN27; -.
DR OrthoDB; 2784069at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR CDD; cd08760; Cyt_b561_FRRS1_like; 1.
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 InterPro; IPR018825; DUF2427.
DR InterPro; IPR018827; YTP1_C.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF10348; DUF2427; 1.
DR Pfam; PF10355; Ytp1; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1262
FT /note="amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007134813"
FT TRANSMEM 58..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..142
FT /note="DUF2427"
FT /evidence="ECO:0000259|Pfam:PF10348"
FT DOMAIN 168..407
FT /note="Protein YTP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10355"
FT DOMAIN 801..1244
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 434..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..456
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..643
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1262 AA; 137178 MW; F96109ADF60C9EFD CRC64;
MARSSSPHPS SPGISIGRLL LFGLVAATLV AAHAHHDAED VGPYEHNFTN EEPLDSIIKW
HIAIQIACWG FLFPVGMVLG ITRSRFHVPW QLVAIALSLA GNYLGHHHHG RGFHMTAHAH
FATYIWWYLM LQLAFGVFLK LHVLEGTTLR RGVVMAHGLL GKSFPVVGWV QMIFGGIAAL
GFCFGDHFGQ CLAHFIMGSA FIGYAMILLL MLRVGAGFLA RKRVSQEYLD SWVIMLWGIV
NTFTEHNFLA AHPTGWSHKD MQHVSLGVLW WAGGALGIFL GRKSTRNVVP AVIIGMTGYA
MANHGQHLEF STDVHKLFGW SLMSAGFARI IEVCFVLRDS ASDNVQPRAF QHLPPYLLVL
SGLTFLSATE EQMQWIAGSG MDSTTYANIL FSGAFAIYLV GNALLELYMV QAQAGGKSPL
RRQHGAIGLA AAATEEDDND DDDRVGLGDD DEDVENAAGA GGPRRYRPTP GLTDSPFPSP
SSSSPIIKRL AHAVPAALAG LVGSVASVVR SLDNAAPSSS SSSSVAGNRE MAEYYESLPL
TNRDSADHHM VQQQQHDHDG HSTLSSSARG AAAQQYPHMN GNNETTTSSH AAGAGRIANG
RRADQRAGAG ASDETVFDIG DFGEDDDDGG DGYWQDDDDD KGVLDDSNGT ARDDEGERVA
GRARSSRHVP AAAASSINAQ GFFSATRRNM ATIGPYHTTL PHITKDDWRD LAAQKREKQA
QLIPAGDDVT GIAEQSGIFS ARELEITDLD EVTELAERIA KQTYTAEEVA VAFSKRAAIA
QQLTNCTSFF RLSSLRHITR LTEIFFKEAI EHAKGLDHIL TKTGKPMDVD GVPVSLKDLF
DIAGTELTQG YVAYLGRISE RDSALVVLLR DSGAVFHCRT NLPQTLMIGD AFNHVFGRTL
NPHCRKLVPG GSSGGEGALI AMKGSILGVG TDIGGSVRIP SAMCGLHTIR PTTRRVPYGH
ATGSFLGQES IVAVAGPMAR SLNSCTYFMR SVLNKNPADY EPTSLPFAFD ESAYERVARD
GKLSFGVMRT DDLVTTAPPI RRALDMAVQR ARDAGHEVIE FDKQDFKKYY ALALKFFSAD
GGEEVRSILA AIDEPLIDGV LVAAEHEKVP SVYALWQLNR AREAMQQKFL DKWLATAKET
STGRPIDGLL TPPAPITACL LGNNRHVGHT TSVQISLFPL AREFSSRKLI LRAFNPEKEL
ADPNFNPLSE EDEKFRGDYD PQLTANVPAA VQLVGRRWRD EELLGLGEIV ADLCGSKNWK
QQ
//
