ID Q2W2U2_MAGSA Unreviewed; 377 AA.
AC Q2W2U2;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN OrderedLocusNames=amb3029 {ECO:0000313|EMBL:BAE51833.1};
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE51833.1, ECO:0000313|Proteomes:UP000007058};
RN [1] {ECO:0000313|EMBL:BAE51833.1, ECO:0000313|Proteomes:UP000007058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007255; BAE51833.1; -; Genomic_DNA.
DR RefSeq; WP_011385405.1; NC_007626.1.
DR AlphaFoldDB; Q2W2U2; -.
DR STRING; 342108.amb3029; -.
DR KEGG; mag:amb3029; -.
DR HOGENOM; CLU_003433_0_0_5; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000007058; Chromosome.
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 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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007058}.
FT DOMAIN 5..358
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 377 AA; 38123 MW; C6A8C31A5F9BD5D8 CRC64;
MSRAVYLDYN SGAPVRPEVA AAMVESLAEP GNPSSVHAFG RAARARVEAA RRQLAGLVGA
DPAGIVFTSG GTEANALALR GCGRSRQLVS AVEHPSVLDA AAEAERIPVT RDGIVDLGAL
ESLLAANTRP ALVSLMLANN ETGIVQPVAE AARIIHAHGA WLHCDAAQAM GRIPVSLRDL
GADILTVSGH KMGGPAGAGA LILAESGRTL APILLGGGQE RRRRAGTENV AGIVGLGVAA
QLAGDDLAGA DTTCGVGALR DRLEQGALRL VPDAAVIGDG APRLPNTTCL VLPGVEGRTQ
VMALDLAGVA VSAGAACSSG KVGPSHVLAA MGLEERVKGS AIRVSLGWSS RPEDVDAFLA
AWVGLARHKG LKVSEAA
//
