ID   CSD_PYRAB               Reviewed;         401 AA.
AC   Q9V242; G8ZG67;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=PYRAB02320; ORFNames=PAB0157;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC         alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64428; EC=2.8.1.7;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000305}.
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DR   EMBL; AJ248283; CAB49156.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69608.1; -; Genomic_DNA.
DR   PIR; E75213; E75213.
DR   RefSeq; WP_010867356.1; NC_000868.1.
DR   AlphaFoldDB; Q9V242; -.
DR   SMR; Q9V242; -.
DR   STRING; 272844.PAB0157; -.
DR   PRIDE; Q9V242; -.
DR   EnsemblBacteria; CAB49156; CAB49156; PAB0157.
DR   GeneID; 1495121; -.
DR   KEGG; pab:PAB0157; -.
DR   PATRIC; fig|272844.11.peg.248; -.
DR   eggNOG; arCOG00065; Archaea.
DR   HOGENOM; CLU_003433_2_5_2; -.
DR   OMA; PVCLRYG; -.
DR   OrthoDB; 24071at2157; -.
DR   PhylomeDB; Q9V242; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   CDD; cd06453; SufS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..401
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150328"
FT   MOD_RES         216
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   401 AA;  44826 MW;  D3B0C619B6C3276F CRC64;
     MRIPEDVRKD IPLTQEVIYF DNTATSLTPK PVIEAMDEYY LRYRANVHRG VHRLSQMATQ
     KYEESRKVVA DFINAEFDEI AFTKNTSESL NLVALGLEHL FKKGDKIVTT PYEHHSNLLP
     WQRLAKKKGL KLEFIEGDDE GNLDLADAEK KIKGAKLVAV QHVSNALGVI HEVEELGKMV
     KEEGAIFVVD AAQSVGHMEV DVKKLKADFL AFSGHKGPMG PTGIGVLYIN KEFFDVFEPP
     LIGGGTIEDV ELCCYKLTEP PERFEAGTPN IGGAIGLAAG IKYIEKIGID KIEKQERKLV
     KRTTEGLDEL EIPWYGPRNL DKHAGVVSFN VPPLHPHDVA SVLDEHKIMV RSGHHCALPV
     MKRLKINGTV RASFHVYNSL EEVETFLGVL EELVKSLRSS Q