CSD_SYNY3
ID CSD_SYNY3 Reviewed; 420 AA.
AC Q55793;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Probable cysteine desulfurase;
DE EC=2.8.1.7;
GN Name=csd; Synonyms=sufS; OrderedLocusNames=slr0077;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-231, AND
RP ACTIVE SITE CYS-372.
RX PubMed=15379559; DOI=10.1021/bi0491447;
RA Tirupati B., Vey J.L., Drennan C.L., Bollinger J.M. Jr.;
RT "Kinetic and structural characterization of Slr0077/SufS, the essential
RT cysteine desulfurase from Synechocystis sp. PCC 6803.";
RL Biochemistry 43:12210-12219(2004).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC produce L-alanine. {ECO:0000250}.
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; BA000022; BAA10545.1; -; Genomic_DNA.
DR PIR; S76601; S76601.
DR PDB; 1T3I; X-ray; 1.80 A; A/B=1-420.
DR PDBsum; 1T3I; -.
DR AlphaFoldDB; Q55793; -.
DR SMR; Q55793; -.
DR IntAct; Q55793; 2.
DR STRING; 1148.1001708; -.
DR DrugBank; DB02346; 3'-O-N-Octanoyl-a-D-Glucopyranosyl-B-D-Fructofuranoside.
DR PaxDb; Q55793; -.
DR EnsemblBacteria; BAA10545; BAA10545; BAA10545.
DR KEGG; syn:slr0077; -.
DR eggNOG; COG0520; Bacteria.
DR InParanoid; Q55793; -.
DR OMA; HKLCGPT; -.
DR PhylomeDB; Q55793; -.
DR BRENDA; 2.8.1.7; 382.
DR EvolutionaryTrace; Q55793; -.
DR Proteomes; UP000001425; 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; 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 TIGRFAMs; TIGR01979; sufS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..420
FT /note="Probable cysteine desulfurase"
FT /id="PRO_0000150318"
FT ACT_SITE 372
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000305|PubMed:15379559"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1T3I"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 65..84
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:1T3I"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1T3I"
FT TURN 207..212
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 285..301
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 303..322
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 352..360
FT /evidence="ECO:0007829|PDB:1T3I"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:1T3I"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:1T3I"
FT HELIX 396..412
FT /evidence="ECO:0007829|PDB:1T3I"
SQ SEQUENCE 420 AA; 46412 MW; B45043D9881AFA23 CRC64;
MVALQIPSLA ATVRQDFPIL NQEINGHPLV YLDNAATSQK PRAVLEKLMH YYENDNANVH
RGAHQLSVRA TDAYEAVRNK VAKFINARSP REIVYTRNAT EAINLVAYSW GMNNLKAGDE
IITTVMEHHS NLVPWQMVAA KTGAVLKFVQ LDEQESFDLE HFKTLLSEKT KLVTVVHISN
TLGCVNPAEE IAQLAHQAGA KVLVDACQSA PHYPLDVQLI DCDWLVASGH KMCAPTGIGF
LYGKEEILEA MPPFFGGGEM IAEVFFDHFT TGELPHKFEA GTPAIAEAIA LGAAVDYLTD
LGMENIHNYE VELTHYLWQG LGQIPQLRLY GPNPKHGDRA ALASFNVAGL HASDVATMVD
QDGIAIRSGH HCTQPLHRLF DASGSARASL YFYNTKEEID LFLQSLQATI RFFSDDDFTV
