ID A0A1G8HBE6_9PSED Unreviewed; 376 AA.
AC A0A1G8HBE6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:SDI03996.1};
GN ORFNames=SAMN05216588_110137 {ECO:0000313|EMBL:SDI03996.1};
OS Pseudomonas flavescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=29435 {ECO:0000313|EMBL:SDI03996.1, ECO:0000313|Proteomes:UP000198606};
RN [1] {ECO:0000313|EMBL:SDI03996.1, ECO:0000313|Proteomes:UP000198606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 18387 {ECO:0000313|EMBL:SDI03996.1,
RC ECO:0000313|Proteomes:UP000198606};
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 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}.
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DR EMBL; FNDG01000010; SDI03996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8HBE6; -.
DR STRING; 29435.SAMN05216588_110137; -.
DR Proteomes; UP000198606; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; 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; 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 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 5..365
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 376 AA; 40085 MW; F5D8D41FC11C1C95 CRC64;
MPELYFDYAA TTPIDDAVIQ DMLACMGRDV VFGNPASASH SFGQRARLAV EKARKQVAAL
VGTTADRLVW TSGATESNNL ALKGVAALAD GRRHIITSRL EHKAVLDTAG QLEREGFEVT
WLQPDANGII QPEAVAAALR DDTLLVSLML INNELGTLTD IAAVGELVRQ RGALFHVDAA
QATGKVAIDL AALPVDLMSF SAHKTYGPKG IGALYVGERA RPLIQAQIHG GGHEQGLRSG
TLATHQIVGM GSAFALAGEL MSEENMRIAR LCAHLREGLL ALPGVRLNGC AEKRVPHTLN
LCIDHPWFDA ENLLGTLAFS STSACNSASS APSHVLLALG LDDTQAYRSI RLSLGRYTTL
ADVEQAIDAI RRCLPE
//
