ID E4UY77_ARTGP Unreviewed; 350 AA.
AC E4UY77;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000313|EMBL:EFR02040.1};
GN ORFNames=MGYG_05042 {ECO:0000313|EMBL:EFR02040.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989825; EFR02040.1; -; Genomic_DNA.
DR RefSeq; XP_003172451.1; XM_003172403.1.
DR AlphaFoldDB; E4UY77; -.
DR STRING; 535722.E4UY77; -.
DR GeneID; 10027721; -.
DR VEuPathDB; FungiDB:MGYG_05042; -.
DR eggNOG; ENOG502QPS1; Eukaryota.
DR HOGENOM; CLU_048897_2_1_1; -.
DR InParanoid; E4UY77; -.
DR OMA; GIQSNHA; -.
DR OrthoDB; 5489296at2759; -.
DR Proteomes; UP000002669; 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:UP000002669}.
FT DOMAIN 18..333
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 56
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 350 AA; 38241 MW; 825EC2370C6AF50F CRC64;
MVKLPETFAA IPREEFLLGP SPIHLLPRTT ADLGGQVKIY AKRDDVSSGL AYGGNKTRKL
EYLAADAVKQ GCDTLVSIGG IQSNHTRQVA AVAARMGLKC GLVQEKWVEW SDPGYEKVGN
IQLSYLMGAD VRIEKMTSFG IEHKDTLKSL MKEYEAKGQK PYYIPAGASD HPFGGVGFAR
WAFEVREQEK EQGITFDYIF VCAVTGSTMA GIVAGFKLIE KLYPDEPKKK IIGIDGSATP
EKTRAQVLRI ARGTAEKIGL KADDITEADI VLDERFHAGT YGVPDKQTWE AIEYGAKMDA
FITDPVYEGK SLAGLLGYVR NGEIKTGNIL YAHLGGQLAL NAYSQLGHVE
//
