ID A0A0V8STK2_9CELL Unreviewed; 384 AA.
AC A0A0V8STK2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=ATM99_12905 {ECO:0000313|EMBL:KSW23573.1};
OS Cellulomonas sp. B6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW23573.1, ECO:0000313|Proteomes:UP000054319};
RN [1] {ECO:0000313|EMBL:KSW23573.1, ECO:0000313|Proteomes:UP000054319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:KSW23573.1,
RC ECO:0000313|Proteomes:UP000054319};
RA Piccinni F.E., Campos E.;
RT "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT Isolated from Decaying Forest Soil.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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:KSW23573.1}.
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DR EMBL; LNTD01000099; KSW23573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V8STK2; -.
DR STRING; 1295626.ATM99_12905; -.
DR Proteomes; UP000054319; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.260.50; -; 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; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054319}.
FT DOMAIN 16..360
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 384 AA; 39247 MW; 8F900CA62353AFDF CRC64;
MRPAALGALT AALARTGNPS SLHTAGRTAR RTVEESRERV AAALGARPSE VVWTAGGTEA
DNLAVKGLFW ARHAQDARRR RVVVSAAEHH AVLDPAFWLA EHSGAELVLL PVDAEGVVEV
DALRSELDEH GDAVALVSVM WANNEVGALQ PLDEVVSLAR RHGVPVHADA VQAVGQVPVD
LAASGVDALT ISGHKVGGPG STGALLLRRG LDVTPVLHGG GQERGVRSGT LDAPLLAAFA
AAVDEAVAER AEHAARVTAL RDDLVRRVLA DVPGATLRGP ADGARRLPAN AHLTFAGCEG
DSLLYLLDAA GVEASTGSAC QAGVPRPSHV LLAMGVGEDD ARGALRFSLG ATSTQDDVDA
AVAALPAAVE RARAAGLTST LVGA
//