ID A0A093ZSJ0_9PEZI Unreviewed; 1511 AA.
AC A0A093ZSJ0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN ORFNames=V491_03843 {ECO:0000313|EMBL:KFY20286.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY20286.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY20286.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY20286.1,
RC ECO:0000313|Proteomes:UP000029338};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KFY20286.1}.
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DR EMBL; JPJT01002206; KFY20286.1; -; Genomic_DNA.
DR HOGENOM; CLU_003782_6_0_1; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000029338; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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 InterPro; IPR013657; SCL35B1-4/HUT1.
DR NCBIfam; TIGR01429; AMP_deaminase; 1.
DR NCBIfam; TIGR00803; nst; 1.
DR PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR Pfam; PF08449; UAA; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029338};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022597}.
FT TRANSMEM 131..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 461..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1460..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1511 AA; 168367 MW; 42FEFC0204D217C3 CRC64;
MASKLTAQIF YANSLVTPEK CREVLWSFFR LGQKEGLSRA LGPIFSWHSA LANPSAPSSS
MLGQVTPRRR ATLRDHLQSS TVDGTEPRPK EINAAPSLEK AQMYGIDNER PTSSKIMALI
GRIFIETIPQ WLAVGVMLGL IFGGCCSNVF ALEAIIKPNP DSGTLLTFVQ FIFIASIGYT
SQFDIKRPPL FLKPNRVPIK RWLVNIALFF TINVLNNHAF SYNISVPIHI ILRSGGSITT
IGVGYMFGKR FSRIQIVSVL LLTVGVIIAA WSDVQSKEKT TDTKQGLPPF SVGLIILFIA
QVLSAIMGLY TEETYREYGP QWKENLFYSH FISLPLFIPF FPSMMRQFLR LAASEPLTMP
WSEPTALGGL PQGFKAGVSG IHIPSQLAYL VVNVLTQYAC IRGVNLLASA SSALTVTIVL
NVRKLVSLLL SIWLFGNRLS FGTLIGATIV FSAGGTVFQG NHPSGQSSPH LEPTRSSVDD
NSDADDNPYH DQDLDESSNS TLADNTTNIA LPGAALDEDL EAEAGTDATQ DGPLPRDFQR
RTTFYDYAAE KQISFTDAKL FYQRSQAEAQ RSGEGGWGSQ QSLPPDSPRL SERKYSNISG
TEVDGPQRSG SLRSIGSGLN MAQSHGKFKS AQPTGLVNPE KSPESNTIQE PVFGSSDGLG
RGNFQRQESR QPENARLPAE LHAAITPEGL HGAGAGIGIG NGAGGFANTE AHVTSELSAI
YANIQKVLDF RHKYMRLSLQ GPEDNPKDDP SWNIYPPHPQ PAWEEEKRRA TMSNGGDSLS
NSTVLPTKAS DKVQAGAANL PQPPNLLKPT RKPGQDIGED FDMEDLLPLP EAGEMTFRLD
DNGVYQVYQH SDAGALEEPV INIPTIREFY MDLEQILEIS SDGPSKSFAF RRLQYLEGKF
NLYVLLNEYQ EMADSKSVPH RDFYNVRKVD THIHHSACMN QKHLLRFIKS KMKKCPNEVV
MFRDGKHLTL SEVFESINLT AYDLSIDTLD MHAHTDSFHR FDKFNLKYNP IGESRLRTIF
LKTDNFIKGR YLAEITKEVI TDLESSKYQM VEWRISIYGR DPDEWDKLAA WVVDNKLFSP
NVRWLVQVPR LYDVYKASGL MDNFEQVVIN VFRPLFEVTK DPSSHPNLHI FLQRVIGFDS
VDDESKVERR LFRKFPVPKV WDTKQNPPYS YWIYYMFANI ASLNVMRKQR GFNTFVLRPH
CGEAGDSDHL AAAVLTCHSI SHGLLLRKVP FLQYIFYLEQ IGVAMSPLSN NALFLAYERN
PFLSYFKRGL NVSLSTDDPL QFAFTKEALI EEYSVAAQIY KLNAVDMCEL ARNSVQQSGY
EASIKQHWLG DNFNKPGVAG NTMAKTNIPN IRQGFRHETL LQEIAMIDRY TSPSTPIPSA
VPSSYETPVG LQSPTSSLKT NLSTTTIPHD QSPFPAQAAR FPHARPTANT SSTSIPPVPM
NLSTDSLQPI NAGLQDLHLS GHEPKFFPGV LSRPQRRDGG EGRPGTERSE KGWEVPVEEE
REDEAGSEEW A
//
