ID A6W7R1_KINRD Unreviewed; 406 AA.
AC A6W7R1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Cys/Met metabolism pyridoxal-phosphate-dependent protein {ECO:0000313|EMBL:ABS02850.1};
GN OrderedLocusNames=Krad_1362 {ECO:0000313|EMBL:ABS02850.1};
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS02850.1, ECO:0000313|Proteomes:UP000001116};
RN [1] {ECO:0000313|Proteomes:UP000001116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC {ECO:0000313|Proteomes:UP000001116};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA Fliermans C., Richardson P.;
RT "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000750; ABS02850.1; -; Genomic_DNA.
DR AlphaFoldDB; A6W7R1; -.
DR STRING; 266940.Krad_1362; -.
DR KEGG; kra:Krad_1362; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_2_11; -.
DR Proteomes; UP000001116; Chromosome.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 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:UP000001116}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 214
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 406 AA; 41508 MW; 929E9B5E110F624E CRC64;
MPENLPADVS ENTPQNAPLS PATLAVVSGR PPRGLDSELN TPVSLSATFV GGGSLGAAEL
GYGRFANPTW AALETAIGDL EGGRALAFAS GMAAVAAALH LVPAEGTVLV PHGAYNGTHS
LSGLLSTQGR LAVQPVDITD LDAVRTALGA LSGPVLLWLE SPTNPLLEVA DIAALAALGH
EHGATVVVDN TFATPLLQRP LELGADVVVH SVTKFLSGHS DVVLGAAVAR DEAVLTALKA
HRTFHGAIPG PMEAFLALRG IRTLPLRLER SQASAADLAR RLLAHPAVTR VRHPSLPDDP
GHALAAAQMA GFGALVSIEV VGGAAGADAV VDAVRLWVPA TSLGGVESLV ERRRRHGNEP
VVVPEDLLRL SVGVEDVEDL WRDLARALDR ALAHAPGSGG GAAGTA
//
