ID   CSD_AERPE               Reviewed;         411 AA.
AC   Q9YAB6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=APE_2023;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000002; BAA81033.1; -; Genomic_DNA.
DR   PIR; A72506; A72506.
DR   AlphaFoldDB; Q9YAB6; -.
DR   SMR; Q9YAB6; -.
DR   STRING; 272557.APE_2023; -.
DR   EnsemblBacteria; BAA81033; BAA81033; APE_2023.
DR   KEGG; ape:APE_2023; -.
DR   PATRIC; fig|272557.25.peg.1350; -.
DR   eggNOG; arCOG00065; Archaea.
DR   OMA; HKLCGPT; -.
DR   Proteomes; UP000002518; 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR010970; Cys_dSase_SufS.
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   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..411
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150325"
FT   MOD_RES         221
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  45293 MW;  7EDBF180D99B1399 CRC64;
     MPRFSCYEVR SEFPELERGI VYLDNAASTL KPRRVVEAMR EFSYRSYANV HRGVHRLSME
     ASKAYEDAHE VVARLVGGSW DEVVFTRNTT EAMQLAALTL AYNGLLRGGE VLVTAADHHS
     TLLPWVRAAR LGGGRARILP LDGRGVPRWD LLEDYITEDT RAVAVGHVSN VTGVVAPVED
     IVKAAKKVGA LVVLDSAQGV PHLPVDFRRM GVDMAAFSGH KMLGPTGIGV LWARRDLLEE
     LEPPLGGGGT VSRVRLQGGS VEIEWEEPPW KFEAGTPPII EAVGLAEAAN MLMEIGMEHV
     ARHEDELTSH TMKLLEPLYS EGLIRYVGPD KPGERHGIVS ITTHLKSPDE LGLLLDRRGI
     AVRTGLHCAH ILHDHVDASM GSVWASFYIY NCKEDAERLA EALEEILTTR R