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Database: UniProt
Entry: M7SAY4_EUTLA
LinkDB: M7SAY4_EUTLA
Original site: M7SAY4_EUTLA 
ID   M7SAY4_EUTLA            Unreviewed;       352 AA.
AC   M7SAY4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative 1-aminocyclopropane-1-carboxylate deaminase protein {ECO:0000313|EMBL:EMR61327.1};
GN   ORFNames=UCREL1_11747 {ECO:0000313|EMBL:EMR61327.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR61327.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate +
CC         NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00001132};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000256|ARBA:ARBA00008639}.
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DR   EMBL; KB707654; EMR61327.1; -; Genomic_DNA.
DR   RefSeq; XP_007799579.1; XM_007801388.1.
DR   AlphaFoldDB; M7SAY4; -.
DR   STRING; 1287681.M7SAY4; -.
DR   KEGG; ela:UCREL1_11747; -.
DR   eggNOG; ENOG502QPS1; Eukaryota.
DR   HOGENOM; CLU_048897_2_1_1; -.
DR   OMA; GIQSNHA; -.
DR   OrthoDB; 5489296at2759; -.
DR   Proteomes; UP000012174; Unassembled WGS sequence.
DR   GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009310; P:amine catabolic process; IEA:InterPro.
DR   CDD; cd06449; ACCD; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR005965; ACP_carboxylate_deaminase.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01274; ACC_deam; 1.
DR   PANTHER; PTHR43780; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   PANTHER; PTHR43780:SF2; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR006278-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012174}.
FT   DOMAIN          25..338
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   ACT_SITE        90
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT   MOD_RES         63
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ   SEQUENCE   352 AA;  37519 MW;  F6B5207F3A9A3EEE CRC64;
     MATTTAAAVV LPEPFASIPR ENFLFGPSPI QALPRISQAL GGKVQVFAKR EDCNSGLAYG
     GNKTRKLEYL ASEALSQGCD TLVSIGGVQS NHTRQVAAVA AKLGLHSALV QEKWVAWEDP
     GYTKVGNIQL ARLMGADSRL DPSAFGIEHK DTLKSMQKEL AAAGRKPYYI PAGASDHPLG
     GLGFARWAFE VQEQERDLGL FFDTVIVCAV TGSTMAGMVA GFKLAEKLGA PKRKVVGIDA
     SATVPQTFDQ VLRIAKATGA KIGLEEGDIT ERDIILDDRY HGGIYGVPDA QTIEAIKFGA
     STEAFITDPV YEGKSLAGMM DMIRKGEIKE GSNVLYAHLG GQLALNAYSS IQ
//
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