ID A0A367YP33_9ASCO Unreviewed; 790 AA.
AC A0A367YP33;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN Name=AMD1_0 {ECO:0000313|EMBL:RCK67584.1};
GN ORFNames=Cantr_03316 {ECO:0000313|EMBL:RCK67584.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK67584.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK67584.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK67584.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004955}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676,
CC ECO:0000256|PIRNR:PIRNR001251}.
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:RCK67584.1}.
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DR EMBL; QLNQ01000001; RCK67584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367YP33; -.
DR STRING; 5486.A0A367YP33; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000253472; Unassembled WGS sequence.
DR GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd01319; AMPD; 1.
DR Gene3D; 4.10.800.20; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01429; AMP_deaminase; 1.
DR PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000253472}.
FT REGION 31..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 92204 MW; C2F1D5F7BDECD567 CRC64;
MTRRSGLNLT MDSGHNVHLL HDNENAIYSH DETEQSDDNE GDDEDDYGHH FNQDSDDEDN
SHLPRSYTSS SFSTSEDKYM KEHDLKMKAF EALHNSNNNG HVPAPQSPGS PKNSFVKRRP
SMIDMPLKFN HIKPPTPNPA LRKNFASDPN ALPEDIPSDE LIDFYSNVKF CLDLRHKYLD
LSLQVPELIN PKNQPGWVIY PAPPKPTYKS KNRFNQLPKE SEDADELEPF DFSKCEIPDL
SDSLFYYELN DEDVYQVYDK ETRKPLVNIP NLHDYYSDVN KIARISSDGP TKSFAFKRLQ
YLEAKWNMYY LLNEFEETKQ SKRNPHRDFY NVRKVDTHIH HSACMNQKHL LRFIKYKLKT
EPDKQVIFRD GKILTLAEVF ESLNLTAYDL SIDTLDMHAH TDTFHRFDKF NLKYNPIGES
RLREIFLKTD NFIDGKYLAE LTTQVMEDLE SSKYQMNELR ISIYGRSIHE WDKLAAWVVD
NKLFSHNVRW LIQVPRLYDI YKKNGNVRSF LDIMKNVFEP LFEVSLNPKS HPKLYVFLQR
VIGFDSVDDE SKTEKPIQSR KYPRASEWSS AMNPPYSYYL YYLYANIASL NHLRMNNKMN
TFVLRPHCGE AGDPEHLISA FLTSYGISHG ILLRKVPFIQ YLYYLDQIGL AMSPLSNNAL
FLTYDKNPFY NFFKKGLNVS LSTDDPLQFS YTKEPLIEEY SVAAQIYKLS GVDMCELARN
SCLQSGWEAQ IKKHWLGKNY LLGGVEGNDI EKTNVPDIRV AFREDTLQCE KDLVNYYNSL
RRSLDSRSSH
//
