ID A0A172TSG7_9BACT Unreviewed; 414 AA.
AC A0A172TSG7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=SY85_04905 {ECO:0000313|EMBL:ANE49932.1};
OS Flavisolibacter tropicus.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavisolibacter.
OX NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE49932.1, ECO:0000313|Proteomes:UP000077177};
RN [1] {ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANE49932.1, ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|EMBL:ANE49932.1,
RC ECO:0000313|Proteomes:UP000077177};
RX PubMed=27259556; DOI=10.1099/ijsem.0.001207;
RA Lee J.J., Kang M.S., Kim G.S., Lee C.S., Lim S., Lee J., Roh S.H., Kang H.,
RA Ha J.M., Bae S., Jung H.Y., Kim M.K.;
RT "Flavisolibacter tropicus sp. nov., isolated from tropical soil.";
RL Int. J. Syst. Evol. Microbiol. 66:3413-3419(2016).
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}.
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DR EMBL; CP011390; ANE49932.1; -; Genomic_DNA.
DR RefSeq; WP_066402078.1; NZ_CP011390.1.
DR AlphaFoldDB; A0A172TSG7; -.
DR STRING; 1492898.SY85_04905; -.
DR KEGG; fla:SY85_04905; -.
DR PATRIC; fig|1492898.3.peg.1073; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000077177; Chromosome.
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; IPR016454; Cysteine_dSase.
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 PIRSF; PIRSF005572; NifS; 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 Reference proteome {ECO:0000313|Proteomes:UP000077177};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 33..402
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 414 AA; 45601 MW; F9049B00AE9DBE89 CRC64;
MIEPAIIETS FDVYAIRQQF PVLNREVKGK PLVYFDNAAT TQKPQVVIDA LVNYYTGYNA
NIHRGIHTLA EEATAAFEAT RDAIKEFVNA ESREQIIFTK GTTEGINLVA QTWGRQNIQA
GDEIIISNME HHSNIVPWYI LCQEKGAVLK VIPISDEGEL DMEAFEKLLS PKTKLVSVVH
VSNALGTINP VKTIIEKAHQ VGALALVDGA QSTVHLDIDV QALGCDFFVF SSHKLYGPTG
MGALYGKKDI LEAMPVYQGG GEMIKEVYFD NIIYNDLPYK YEAGTPNIAD AIAFKSALDF
TKGIGKENIR QHENELLAYA TAQLEAIPGL RIIGQAKQKI SVISFVIDNV HPQDIGILLD
NRGIAVRTGN HCAQPLMDRL CIRGTTRASF AMYNTKEEVD VLIAGLQKAI KLLA
//
