ID A0A1H5PCZ2_9ACTN Unreviewed; 418 AA.
AC A0A1H5PCZ2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=SAMN05216533_6531 {ECO:0000313|EMBL:SEF11802.1};
OS Streptomyces sp. Ag109_O5-10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEF11802.1, ECO:0000313|Proteomes:UP000198812};
RN [1] {ECO:0000313|EMBL:SEF11802.1, ECO:0000313|Proteomes:UP000198812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEF11802.1,
RC ECO:0000313|Proteomes:UP000198812};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- 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; FNTQ01000001; SEF11802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5PCZ2; -.
DR STRING; 1855349.SAMN05216533_6531; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000198812; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
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; IPR010970; Cys_dSase_SufS.
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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000198812}.
FT DOMAIN 31..406
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 418 AA; 45796 MW; 697B0F6ACB1FBFD1 CRC64;
MTQLPGLLDT EAIRKDFPVL DRLVHDGKKL VYLDNAATSQ KPRQVLDVLS EYYERHNANV
HRGVHVLAEE ATAMYEGARD KVAEFINAPS RDEVIFTKNA SESLNLVANM LGWADEPYRV
DHETEIVITE MEHHSNIVPW QLLAQRTGAK LKWFGLTDDG RLDLSNIDEV ITEKTKIVSF
VLVSNILGTV NPVEAIVRRA QEVGALVCVD ASQAAPHMPL DVQALQADFV AFTGHKMCGP
TGIGVLWGRQ ELLEDLPPFL GGGEMIETVS MHSSTYAPAP HKFEAGTPPI AQAVGLGAAI
DYLGAIGMDK ILAHEHALTE YAVQRLQQVP DLRIIGPTTA EDRGAAISFT LGDIHPHDVG
QVLDEQGIAV RVGHHCARPV CLRYGIPATT RASFYLYSTP AEIDALVEGL EHVRNFFG
//
