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Database: UniProt
Entry: K9QSY5_NOSS7
LinkDB: K9QSY5_NOSS7
Original site: K9QSY5_NOSS7 
ID   K9QSY5_NOSS7            Unreviewed;       327 AA.
AC   K9QSY5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000313|EMBL:AFY48518.1};
GN   OrderedLocusNames=Nos7524_2685 {ECO:0000313|EMBL:AFY48518.1};
OS   Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY48518.1, ECO:0000313|Proteomes:UP000010378};
RN   [1] {ECO:0000313|Proteomes:UP000010378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003552; AFY48518.1; -; Genomic_DNA.
DR   RefSeq; WP_015138956.1; NC_019684.1.
DR   AlphaFoldDB; K9QSY5; -.
DR   STRING; 28072.Nos7524_2685; -.
DR   KEGG; nop:Nos7524_2685; -.
DR   PATRIC; fig|28072.8.peg.2946; -.
DR   eggNOG; COG2515; Bacteria.
DR   HOGENOM; CLU_048897_0_0_3; -.
DR   OrthoDB; 9801249at2; -.
DR   Proteomes; UP000010378; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010378}.
FT   DOMAIN          15..293
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   ACT_SITE        66
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT   MOD_RES         39
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ   SEQUENCE   327 AA;  36398 MW;  B08C49196A4D35EB CRC64;
     MLHSPIPTQQ INSEIANCAG VEMYVLRLDL MHPWVNGNKW FKLKYNLLAA KEENFTTLLT
     FGGAYSNHIY ATAAAGNLFG FRTIGVIRGE ERLPLNPTLS FAVQQGMQLM YVDRETYRQR
     HTPELHAQLR QRFGEVFMIP EGGCNLNGVR GCTEILAEVT AIFNTVCMAC GTATTLIGLT
     LASPSAKKIL GFPVLKNGEF LKQDINNLLT QYLASGLPAP SLTPTPWELI CNYHFGGYAK
     VNDHLLAFSQ EFTQTYGIPL DYVYTAKMFY GVIDLIQQGF FARGDRLLLI HTGGLQGNLG
     MRERLKNLPV LFRNEASEMS LTGSISN
//
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