ID A5EYF2_DICNV Unreviewed; 404 AA.
AC A5EYF2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN Name=sufS {ECO:0000313|EMBL:ABQ13769.1};
GN OrderedLocusNames=DNO_0834 {ECO:0000313|EMBL:ABQ13769.1};
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195 {ECO:0000313|EMBL:ABQ13769.1, ECO:0000313|Proteomes:UP000000248};
RN [1] {ECO:0000313|EMBL:ABQ13769.1, ECO:0000313|Proteomes:UP000000248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A {ECO:0000313|EMBL:ABQ13769.1,
RC ECO:0000313|Proteomes:UP000000248};
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from the
RT animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
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 Evidence={ECO:0000256|ARBA:ARBA00001357};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily.
CC {ECO:0000256|ARBA:ARBA00010447}.
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DR EMBL; CP000513; ABQ13769.1; -; Genomic_DNA.
DR RefSeq; WP_012031157.1; NC_009446.1.
DR AlphaFoldDB; A5EYF2; -.
DR STRING; 246195.DNO_0834; -.
DR KEGG; dno:DNO_0834; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_5_6; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000000248; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; 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 NCBIfam; TIGR01979; sufS; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ABQ13769.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000000248}.
FT DOMAIN 23..392
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 404 AA; 44071 MW; FF7C8756F4536EA8 CRC64;
MNADIRAEFP ILQEKNGGKR LAYLDNAASV HKPLAVMAAM DQCLKKEYSN IHRGVHWLSQ
RLTQRYETVR EKVASFLHAE RVDEIIFTKG TTDSLNLLAS SLSELLLKSG DKVLITAMEH
HANIVPWQIA CRKAGAQLVV LPMDERGVLE AQHLPDLLSG VKIFSITQVS NALGTINPVK
ALIQKVKAFN PDIVCIVDGA QAVAHLPVDV QDLGCDFYAF SAHKLYGPTA VGVLYGRYDL
LEAMPPYQSG GDMILSVSFE KTSYAPPPHK FEAGTPPIVE VIGLGAAIDW VQSVGLSSIQ
NWEQQLHAQA EKALMDFSGV RIYGTAPEKA AVISFTLNGI HPHDAGTIFD AQGVAVRVGH
HCAEPVMRFF HIPATIRASF AVYNDEADVA QLLAAVRATQ EMFA
//
