ID J2WSV2_9SPHN Unreviewed; 401 AA.
AC J2WSV2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN ORFNames=PMI04_00950 {ECO:0000313|EMBL:EJK85335.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK85335.1, ECO:0000313|Proteomes:UP000006480};
RN [1] {ECO:0000313|EMBL:EJK85335.1, ECO:0000313|Proteomes:UP000006480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK85335.1,
RC ECO:0000313|Proteomes:UP000006480};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:0000256|RuleBase:RU004506}.
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 ECO:0000256|RuleBase:RU004506};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000256|ARBA:ARBA00010447,
CC ECO:0000256|RuleBase:RU004506}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJK85335.1}.
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DR EMBL; AJVL01000016; EJK85335.1; -; Genomic_DNA.
DR RefSeq; WP_007706736.1; NZ_CP124576.1.
DR AlphaFoldDB; J2WSV2; -.
DR STRING; 1144307.PMI04_00950; -.
DR PATRIC; fig|1144307.3.peg.910; -.
DR eggNOG; COG0520; Bacteria.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000006480; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
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; 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 NCBIfam; TIGR01979; sufS; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF8; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 21..389
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 401 AA; 42946 MW; 119A0062B370D85A CRC64;
MTDLAQGLRL RDDFPGVGNW HYLDSAATAQ KPTAVIDAIA RAYGPDYATV HRGVYERSAN
MTLAYEAARR KVAGFIGAAS DSEIVYVRGA TEGINLVAQC WAGTQLKAGD RILLSTLEHH
SNIVPWQIVA EKVGAHIDVV PLTEDGRIDL DAMRAMITPQ HRMVALAHVS NVLGSVLDCR
RAADIAHMVG AKILIDGCQA VPRLAVDVAA LDCDFYVFSA HKLYGPTGIG VLWGRKKLLD
IMPPYQGGGS MIDKVTFEKT TYAPAPTRFE AGTPHIVGVV GLSAAIDYVQ GIGLDAIHAH
ECAMVAKART AISQINSVRV FGPEDSAGIL SFEVEGVHPH DVGTILDETG VAIRAGHHCA
QPLMRHLGVE ATARASFGIY SDDSDVDALV KGIERVRKIF G
//