ID D5ZYT4_STRV1 Unreviewed; 305 AA.
AC D5ZYT4;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000313|EMBL:EFE67187.2};
GN ORFNames=SSFG_02436 {ECO:0000313|EMBL:EFE67187.2};
OS Streptomyces viridosporus (strain ATCC 14672 / DSM 40746 / JCM 4963 / KCTC
OS 9882 / NRRL B-12104 / FH 1290) (Streptomyces ghanaensis).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE67187.2, ECO:0000313|Proteomes:UP000003824};
RN [1] {ECO:0000313|Proteomes:UP000003824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14672 / DSM 40746 / JCM 4963 / KCTC 9882 / NRRL B-12104 /
RC FH 1290 {ECO:0000313|Proteomes:UP000003824};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces ghanaensis ATCC 14672.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; DS999641; EFE67187.2; -; Genomic_DNA.
DR RefSeq; WP_004983550.1; NZ_DS999641.1.
DR AlphaFoldDB; D5ZYT4; -.
DR eggNOG; COG2515; Bacteria.
DR Proteomes; UP000003824; Unassembled WGS sequence.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
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}.
FT DOMAIN 30..301
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 54
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 305 AA; 32158 MW; BD617A850F7EE81B CRC64;
MTSSDDPGST ALTGLRPRLP SPLQEVTDER FARRGIRLLL KRDDLIHPEL VGNKWRKLAP
NLAAAGGRTV LTFGGAYSNH LRATAAAGRL LGLRTVGVVR GQELAGRPLN PSLARCVSDG
MRLHFVDRST YRRKTEPETL AAVLRAADAE AAYVVPEGGS NSLAVRGCRT LGAELAGRAD
VVAVACGTGG TLAGLAAGLG TGGRALGVPV LKGGFLADVT RALQDEAFGG PRGDWSLDDR
FHFGGYARVP EELDAFAEDF EHRHGIPVER LYVAKLLHAL VALAEEGAFP RGSTVAAVIT
GRPFP
//
