ID   G0SDU6_CHATD            Unreviewed;       354 AA.
AC   G0SDU6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative 1-aminocyclopropane-1-carboxylate protein {ECO:0000313|EMBL:EGS18697.1};
GN   ORFNames=CTHT_0053040 {ECO:0000313|EMBL:EGS18697.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS18697.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL988045; EGS18697.1; -; Genomic_DNA.
DR   RefSeq; XP_006695642.1; XM_006695579.1.
DR   AlphaFoldDB; G0SDU6; -.
DR   STRING; 759272.G0SDU6; -.
DR   GeneID; 18259342; -.
DR   KEGG; cthr:CTHT_0053040; -.
DR   eggNOG; ENOG502QPS1; Eukaryota.
DR   HOGENOM; CLU_048897_2_1_1; -.
DR   OMA; GIQSNHA; -.
DR   OrthoDB; 5489296at2759; -.
DR   Proteomes; UP000008066; 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:UP000008066}.
FT   DOMAIN          20..341
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT   MOD_RES         59
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ   SEQUENCE   354 AA;  38428 MW;  392CFB85E72A306C CRC64;
     MVVKVELPEP FVSIPREPLT FGPSPIQHLP RISQALGGKV NVYAKREDCN SGLAFGGNKI
     RKLEYLLPDA LAQNCDTLIS IGGIQSNHTR QVAAAAAKLG LHVALVQEHW VPGVWSANPV
     YSRVGNLQLS RLIGADVRVA SPEEGFGIQH KPTLARLREK LIAEGKKPYY IPAGASDHPL
     GGLGFARWAF EVIAQEEEME VFFDTVVVCA VTGSTFAGMV AGFKLAELKL GARKRRVVGI
     DASAKPAETR EQVLRIARQT AVRIGLEEGD IQDEDVVLDE RYHAGAYGVP DERTMEAIRF
     GARTEAFITD PVYEGKSFAG MLDMIRNGEM PEGSNVLFAH LGGQLALNAY SALE
//