ID C5DWD1_ZYGRC Unreviewed; 767 AA.
AC C5DWD1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 13-SEP-2023, entry version 69.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN OrderedLocusNames=ZYRO0D13838g {ECO:0000313|EMBL:CAR28100.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR28100.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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}.
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DR EMBL; CU928176; CAR28100.1; -; Genomic_DNA.
DR RefSeq; XP_002497033.1; XM_002496988.1.
DR AlphaFoldDB; C5DWD1; -.
DR STRING; 559307.C5DWD1; -.
DR GeneID; 8204296; -.
DR KEGG; zro:ZYRO0D13838g; -.
DR HOGENOM; CLU_003782_2_2_1; -.
DR InParanoid; C5DWD1; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000008536; Chromosome D.
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:UP000008536}.
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 88629 MW; 3C671F705B00DF25 CRC64;
MDADSSYKNL ADLSLEPTES HDVANPESAG LFAGNDKPER VSEGVALAPS EADAHFSYKE
NKELLERGTK ELAVDHQAPS NFNQPSGLEN DSPHSKKDRA LSSSAKLTVP DLPTDTHRGA
RRSSTYKMGV FADDSTQRFL DEPSPELVGL YSNVAECRAM REKYQTTSLQ HDWDNPKNKP
DWLIYPPPPR PTYNPETKTV TKLENRPDCE VFDFEKCVIP GEDTDYDFGV GGDDIYVVHS
AQDSAKLVSK VPDLREYYMD LERVIALSSD GPAKSFAFRR LQYLEARWNL YYLLNEFQET
SVSKRNPHRD FYNVRKVDTH VHHSACMNQK HLLRFIKHKL RHNGEEDVIF RDGKILTLDQ
VFKSLNLSGY DLSIDTLDMH AHKDTFHRFD KFNLKYNPIG ESRLREIFLK TDNYVKGSYL
AQVTKEVVSD LENSKYQNCE YRISVYGRSI DEWDKLASWV IDNKLISHNV RWLIQCPRLY
SIYKSTGQVE NFFDLMRNIY QPLFEVTKNP QSHPKLHVFL QRVIGFDSVD DESKVDRRIF
RKYPKASNWD NPNNPPYSYY LYYMYASMAS LNQWRAKRGF NTLVLRPHCG EAGDPEHLVS
AYLVAQSISH GILLRKVPFV QYLYYLDQVG IAMSPLSNNA LFLTYDKNPF PHYFKRGLNV
SLSTDDPLQF SYTREPLIEE YSVAAQIYKL SNVDMCELAR NSVLQSGWEA QIKSHWIGKD
FYKNGVEGND VGKTNVPNIR INYRWDTLST ELELMNHFSN FKDAIED
//
