ID Q9RVV1_DEIRA Unreviewed; 392 AA.
AC Q9RVV1;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 08-NOV-2023, entry version 115.
DE SubName: Full=Trans-sulfuration enzyme {ECO:0000313|EMBL:AAF10498.1};
GN OrderedLocusNames=DR_0921 {ECO:0000313|EMBL:AAF10498.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF10498.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF10498.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE000513; AAF10498.1; -; Genomic_DNA.
DR PIR; D75458; D75458.
DR RefSeq; NP_294645.1; NC_001263.1.
DR RefSeq; WP_010887566.1; NZ_JMLF01000010.1.
DR AlphaFoldDB; Q9RVV1; -.
DR STRING; 243230.DR_0921; -.
DR PaxDb; 243230-DR_0921; -.
DR EnsemblBacteria; AAF10498; AAF10498; DR_0921.
DR GeneID; 69517164; -.
DR KEGG; dra:DR_0921; -.
DR PATRIC; fig|243230.17.peg.1108; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_0; -.
DR InParanoid; Q9RVV1; -.
DR OMA; MQTKLIH; -.
DR OrthoDB; 54490at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR CDD; cd00614; CGS_like; 1.
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:SF85; 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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 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:UP000002524}.
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 392 AA; 42095 MW; 8825EA6513009BA5 CRC64;
MDNSARFRTR AVHAGHGLDP ATGAHAMPIY ATSTFGYGDA ARGQRLFAGE EQGHFYSRLS
NPTVRAFEEK LASLEGTEDA LAFASGMGAA SAILLTLLRS GDEVAFLAPL YGGTEGLLQD
MLPKFGIRVW EAKDPADLRG RLTDRTRLVW LETPSNPTLR LTDLREVADL AHGAGARLVV
DNTFSTPYLT RPAEFGADLV MHSATKYLGG HGDVIGGVVA GDAATLLDLR LHGLRHVGAS
LGPFEAYLLL RGMKTLPLRM EAHCAGAHLI AERLAARGDL KVYYPGLPEH PGHDLARRQM
SGRFGGIVSL DLGDFAAAQQ FLDALQLFTQ AVSLGDVESL SSHPASTTHQ LLGEEVLNAH
GIVPGLVRLS VGIEDPEDLW ADIEQALRQA RR
//