ID Q6AN40_DESPS Unreviewed; 332 AA.
AC Q6AN40;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Probable 1-aminocyclopropane-1-carboxylate deaminase {ECO:0000313|EMBL:CAG36234.1};
GN OrderedLocusNames=DP1505 {ECO:0000313|EMBL:CAG36234.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG36234.1, ECO:0000313|Proteomes:UP000000602};
RN [1] {ECO:0000313|Proteomes:UP000000602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG36234.1; -; Genomic_DNA.
DR RefSeq; WP_011188746.1; NC_006138.1.
DR AlphaFoldDB; Q6AN40; -.
DR STRING; 177439.DP1505; -.
DR KEGG; dps:DP1505; -.
DR eggNOG; COG2515; Bacteria.
DR HOGENOM; CLU_048897_1_0_7; -.
DR OrthoDB; 9801249at2; -.
DR Proteomes; UP000000602; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005966; D-Cys_desShydrase.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01275; ACC_deam_rel; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR006278-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000602}.
FT DOMAIN 12..319
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 50
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 332 AA; 35575 MW; 936567F626D94DD4 CRC64;
MNLTQFPRRN YLQGPTPIEA APRFSKALGG KVNVFIKRDD LLPGCAGGNK TRKLDFCIAD
AIEKGADTII TCGPVQSNHC RLTLSWAVKE EMDCHLILEE RVPGSYKEDG SGNNFLFNLM
GVKSTQVVPG GSDMMGEMEK LAKELEAQGK KPYIIPGGAS NVLGATGYVA CAQEIQQQLF
QQNINITDIV VPSGSAGTHA GVAVGMYGIN SGIRVSGINV SKPKDVQEEN VYKLAYETAK
AVGVCGELPR GEITCFDGYV GAGYSLPTDS MVEAVKLLAR TEAILLDPVY SGKVMAGMID
LIRNDYFAPG TNVLFLHTGG SPALYAYTDT FK
//
