ID A0A0A6RXJ9_9GAMM Unreviewed; 375 AA.
AC A0A0A6RXJ9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 2.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=PN36_02660 {ECO:0000313|EMBL:KHD08616.2};
OS Candidatus Thiomargarita nelsonii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiomargarita.
OX NCBI_TaxID=1003181 {ECO:0000313|EMBL:KHD08616.2, ECO:0000313|Proteomes:UP000030428};
RN [1] {ECO:0000313|EMBL:KHD08616.2, ECO:0000313|Proteomes:UP000030428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hydrate Ridge {ECO:0000313|EMBL:KHD08616.2};
RX PubMed=27199933; DOI=10.3389/fmicb.2016.00603;
RA Flood B.E., Fliss P., Jones D.S., Dick G.J., Jain S., Kaster A.K.,
RA Winkel M., Mussmann M., Bailey J.;
RT "Single-Cell (Meta-)Genomics of a Dimorphic Candidatus Thiomargarita
RT nelsonii Reveals Genomic Plasticity.";
RL Front. Microbiol. 7:603-603(2016).
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:KHD08616.2}.
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DR EMBL; JSZA02000007; KHD08616.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6RXJ9; -.
DR Proteomes; UP000030428; 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; IPR017644; Cysteine_desulfurase_DndA.
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; TIGR03235; DNA_S_dndA; 1.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000030428}.
FT DOMAIN 5..359
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 375 AA; 40645 MW; 5D555A3C17A085D4 CRC64;
MPMTTYLDCN ATTPMEPAVC DAVLKYMTTE FGNAGSRTHE FGGRAKQAVQ NARDKIAEMV
AASREEVIFT SGATESNNLA ILGLKTYGEQ NAKKHIVSTQ IEHKAVLEPL AILKKSGFDV
TLVPPTKGGW VEPDAIKDAV RDDTLLVSVM HVNNETGIIQ PLAEIAERLA THPAYFHVDA
AQGFGKDIPT LRHPRIDLIS ASSHKIYGPK GVGTLIVRRR AYQKVPLTAL MYGGGQERGL
RPGTLPVHLI VGFGVATELA LKQAEKRANI CRVFRDQVLE GLAPLKPVIH GDPARCLPHV
INFSVDGLDS EAAMLALKGL VAISNGSACT SSSYTPSHVL KAMGEIQGSL RMSWCHRTEQ
VNWAEIVKCL NRILS
//