ID A0A176U6U5_9FIRM Unreviewed; 380 AA.
AC A0A176U6U5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=HMPREF2738_01538 {ECO:0000313|EMBL:OAD88473.1};
OS Clostridiales bacterium KLE1615.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1715004 {ECO:0000313|EMBL:OAD88473.1, ECO:0000313|Proteomes:UP000077212};
RN [1] {ECO:0000313|EMBL:OAD88473.1, ECO:0000313|Proteomes:UP000077212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1615 {ECO:0000313|EMBL:OAD88473.1,
RC ECO:0000313|Proteomes:UP000077212};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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. Csd subfamily.
CC {ECO:0000256|ARBA:ARBA00010447}.
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:OAD88473.1}.
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DR EMBL; LXPQ01000111; OAD88473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176U6U5; -.
DR PATRIC; fig|1715004.3.peg.1532; -.
DR Proteomes; UP000077212; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; IPR010969; Cys_dSase-rel_unknwn_funct.
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; TIGR01977; am_tr_V_EF2568; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF4; ISOPENICILLIN N EPIMERASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000077212}.
FT DOMAIN 2..367
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 380 AA; 41450 MW; E5F21FDA5463821E CRC64;
MIYLDNAATS LQKPKEVEEE MIRALHTMGN PGRGAHDATL QAGRCVYQVR EQLAQLFKAE
SADCIAFTSN ATEALNTAIL GLFQKGDHVI TTVCEHNSVL RPLYRLQKQG VEVSFLSADE
QGILDYDKLP ALIKENTKAV IVTHASNLTG NITDLECIKK EISQKDILFI ADASQTAGIL
PIDVQKMGID VLCFTGHKGL MGPQGTGGLY VRQGVKINPL KVGGSGIHSF DHEHPKAMPE
HLEAGTLNVH GIAGLGGALN YLSEIGTEAI IKKERSLIKR LEDQIRDLPN IHLYGNPDSS
QRVGILSFNM GDEDSAYVAD WLFEEKEIAV RSGAHCAPLM HEALGTKMQG AVRISVSHKN
TEEEIDRTAN AIKKLSQLLE
//
