ID F5R8K5_METUF Unreviewed; 379 AA.
AC F5R8K5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:EGK73383.1};
GN ORFNames=METUNv1_00561 {ECO:0000313|EMBL:EGK73383.1};
OS Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / FAM5).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1000565 {ECO:0000313|EMBL:EGK73383.1, ECO:0000313|Proteomes:UP000005019};
RN [1] {ECO:0000313|EMBL:EGK73383.1, ECO:0000313|Proteomes:UP000005019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5
RC {ECO:0000313|Proteomes:UP000005019};
RX PubMed=21725020; DOI=10.1128/JB.05331-11;
RA Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., Medigue C.,
RA Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., Kalyuzhnaya M.G.;
RT "Genome sequence of Methyloversatilis universalis FAM5T, a methylotrophic
RT representative of the order Rhodocyclales.";
RL J. Bacteriol. 193:4541-4542(2011).
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 -!- 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:EGK73383.1}.
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DR EMBL; AFHG01000029; EGK73383.1; -; Genomic_DNA.
DR RefSeq; WP_008058595.1; NZ_AFHG01000029.1.
DR AlphaFoldDB; F5R8K5; -.
DR STRING; 1000565.METUNv1_00561; -.
DR eggNOG; COG1104; Bacteria.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000005019; 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 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:UP000005019}.
FT DOMAIN 5..359
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 379 AA; 39095 MW; EA38CC685A41B552 CRC64;
MFAPVYLDHN ASAPLLDAVR EAMLPWLGAR FGNASSRHEY GRAARRAIDD ARARVAAAVG
AHPTEVVFTS GGSEANNLFI KGAAARMKPG LVQVSAIEHP CVREPARQLV RAGWTLAEMP
ADADGRVELD ALDVRAQLVS VMAANNETGV LQDISAFATA AKRQGAWLHT DAVQALGKIP
VDFRALGVAA MTLSAHKIGG PQGAGALVLD KRVDLEPLIA GGGHERGLRS GTENIAAIVG
FGVACEEAVA ALGARREAMQ AQRALIERCV AEQGGSVFGA GAERLPNTCY FALPGIDGET
LVGKLDRAGF AVASGAACSS ASPEPSRTLT AMGVAADLAR GAVRVSVGAS TTMQDVNDFC
GALARVADEL RGLRAMAAA
//