ID A0A1E3I9T1_9TREE Unreviewed; 996 AA.
AC A0A1E3I9T1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN ORFNames=L202_00462 {ECO:0000313|EMBL:ODN84531.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN84531.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN84531.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN84531.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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 -!- 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:ODN84531.1}.
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DR EMBL; AWGJ01000001; ODN84531.1; -; Genomic_DNA.
DR RefSeq; XP_018998334.1; XM_019133629.1.
DR AlphaFoldDB; A0A1E3I9T1; -.
DR STRING; 1295533.A0A1E3I9T1; -.
DR GeneID; 30151771; -.
DR OrthoDB; 20951at2759; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000094065; 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 SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000094065}.
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 112608 MW; 7D61B82BBA854635 CRC64;
MDDSSPPSPL PDPLPIPTTA YRRHQDLEDH EHSSPAFDYH QERRLHLKDE IWMSHHLPRL
PPTSVSEAGS SVRTETGTSY KNKMAPGDYL EFTSPSARVR QLSPKASFKN ITQPEFGNVA
RGGDGMALDD TQEAPNEEED FAGAFQRRAS IQPEPQSTLL SPSGPEYGDL DPAASIIHRQ
ERDQQEALDL EEERKEKELA LKGLAGIEGG QLSQKAPQEA PKEHLPVEHG IGNELESLYA
SFSRCLELRD KYLELSNQRL GDNPRDHDGT FHGFNPPSAA DVTGLKPEYD PASSELPPDA
KDALPAWNIY PPPPPPHWHW KKADNGPLPE PAPLTTEGEE ENDGKKAKGV SSKDSEVFDV
ADCQIPGRDP TGWTYELNDE GVFTVFAAEP ASAEATPVKE GEAPQRKISL SRVPTLKEYF
TDLDYLLGVC SDGPAKSFAF RRLKYLQSKW SLYCLLNEYQ ELADMKAVPH RDFYNVRKVD
THIHHSASMN QKHLLRFIKS KLRKSPDEIV IHRDGKELTL KEVFQSLDLT AYDLSIDMLD
MHAHQEFHRF DRFNDRYNPT GSSRLREIFL KTDNLLKGKY LAELTQELIT DLEQSKYQQS
EWRLSIYGRN VNEWDKLAKW VVNHKLISHN VRWLIQVPRL YEVYKGQGLV NNFEDVVKNI
FGPLFEVTQD PSSHPELHIF LQRVVGFDSV DDESKPERRL YRKFPTAKMW DTKQSPPYSY
WIYYMYANMA SLNAWRRSRN FNTFVLRPHC GEAGDPDHLS SAFLTAHSIS HGILLRKVPA
LQYLFYLKQI GLAMSPLSNN ALFLTYERNP FKDFFRTGLN VSLSTDDPLQ FHFTASHLLE
EYSCAAQIYK LTPADMCELA RNSVLQSGWE MQVKKHWIGQ HWYLPGAAGN DIHKTNVPTI
RLAYRQATLL EELALIRHGK HSPSATPTHL KPRTETTVAI PERPGMTTHA SDVGAAAMSM
SAGVGTAGVG APNGSHLVGG ASELDQRSLE KQRGQQ
//
