ID A4FLT4_SACEN Unreviewed; 450 AA.
AC A4FLT4;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=SACE_5825 {ECO:0000313|EMBL:CAM05009.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM05009.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM05009.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
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}.
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DR EMBL; AM420293; CAM05009.1; -; Genomic_DNA.
DR AlphaFoldDB; A4FLT4; -.
DR STRING; 405948.SACE_5825; -.
DR KEGG; sen:SACE_5825; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_0_11; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000006728; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; 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 Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW Transferase {ECO:0000313|EMBL:CAM05009.1}.
FT DOMAIN 42..412
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 450 AA; 47655 MW; 869B5890236C169B CRC64;
MATRPFQIPE QSVVDTAARV PAVVGEALRV PLVTGGRIGY ANLDHAASAP CLRSVRDAVD
ELLPWYASVH RGAGFASQVC TRVYEGARAK LRAFTGARDT DAVVFTRNTT DALNLLAKAL
PRATSVVVFD TEHHAALLPW GSGPRVRRLP APATPEDAVE ALDAALAACP EGPRLAVLTG
ASNVTGEVWP VAELARVARR RGARTVLDAA QLAPHRPVRI GELDIDYVAI SGHKLYAPFG
AGALVGRADW LNAADPYLAG GGATRAVRDS SVGWNLGPER HEAGSPNTVG VHALAAACQT
LAADGWRPVI EHEALLLRRL RAGLGEVPGL RELSLFGTGH DRVGVVSFTV DGRDPGLLAA
ALSAEHGIGV RDGLFCAHLA MQRLLAESGA DSQRALRVSV GLGTMTEHVD RLVAALHRLV
AEGPRWRYEQ VDGRWVPVDD PREAPAFLDG
//
