ID Q7VTK3_BORPE Unreviewed; 414 AA.
AC Q7VTK3;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 08-NOV-2023, entry version 92.
DE SubName: Full=Cys/Met metabolism PLP-dependent enzyme {ECO:0000313|EMBL:CAE43787.1};
GN OrderedLocusNames=BP3528 {ECO:0000313|EMBL:CAE43787.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE43787.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; BX640421; CAE43787.1; -; Genomic_DNA.
DR RefSeq; NP_882043.1; NC_002929.2.
DR RefSeq; WP_010931523.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VTK3; -.
DR STRING; 257313.BP3528; -.
DR PaxDb; 257313-BP3528; -.
DR GeneID; 69600474; -.
DR KEGG; bpe:BP3528; -.
DR PATRIC; fig|257313.5.peg.3820; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_4; -.
DR OMA; MQTKLIH; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF80; GAMMA-CYSTATHIONASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002676}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 414 AA; 44881 MW; BD81989EAF2CA1E6 CRC64;
MHQNGFTTTI VHSDRDQSAE HGAVHKPMHP SSEYVYEDAR ELAAVFQGKA GFTYARQGTP
TTTALEARIT RMEAGKSTVS FATGMAALAA IFTTLLRRGD HLVSSQYVFG NTNSLLNTLM
ELGVEVTMVD ATDVRQVRDA LRPNTRMVFT ETIANPGTQI ANLAGMGALC RERGLVYVVD
NTLTSPWMFR PVEVGASLVM NSLSKYIAGH GHALGGAVTD TGLYDWSGYA NIYESYRKGA
PTGWGLTQIK KKGLRDMGGT LAAEPAHRIA IGTETLALRM ARHCSNALAL ATFLQGHPGV
ARVHYPGLSS HAQHQRASEL FDGRYGGLLG VELAEGIDCF DFLNRLRIVL MATHLGDTRS
LALPAAHTIY YEMGAEKRAQ MGIADSLIRV SVGIEDEADL LFDFDQALRG CLQS
//