ID A0A254RCN2_9BACT Unreviewed; 413 AA.
AC A0A254RCN2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=B7994_09635 {ECO:0000313|EMBL:OWU99923.1};
OS Fibrobacter sp. UWR2.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1964352 {ECO:0000313|EMBL:OWU99923.1, ECO:0000313|Proteomes:UP000197391};
RN [1] {ECO:0000313|EMBL:OWU99923.1, ECO:0000313|Proteomes:UP000197391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWR2 {ECO:0000313|EMBL:OWU99923.1,
RC ECO:0000313|Proteomes:UP000197391};
RA Neumann A.P., Suen G.;
RT "Draft genomes of novel Fibrobacter strains.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:OWU99923.1}.
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DR EMBL; MWQE01000006; OWU99923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254RCN2; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000197391; 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; 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:UP000197391};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 31..401
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 413 AA; 45258 MW; 659336C50D85FE79 CRC64;
MDNSNIFNAE AVRGEFPMLV AGDKGAKPLA FLDSTATTQK PACVIDAMDD FYREHYSSVK
RGVYRLSART TEAFEATRKN VAKFINAKTE DEIVFTRGTT ESINLVAWSY GRKFFEAGDE
ILISGLEHHA NIVSWQLVAE MKGAKIKVIP VKDDGDLDLD KLPGLLNART KMVAVTHVSN
AVGTVNPIAE IIKTVRAAAP QAKILIDGAQ SSSHIKIDVQ ALDCDFLAFS GHKMYGPTGV
GVLYGKYDVL DSMPPWHGGG EMIKNVTFEK TTYADVPARF EAGTPMIAEV IGLGKAIEWI
NEKGIENIRK HEEEITQYAL EQLAQIPQVK IFGNPKERGA LVSITLDGIA VSDAAMILDE
ENVAVRSGHH CAQPVMDRFG VDATLRLSFG AYTLKRDIDR FVAGIKRVVR LFA
//
