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Database: UniProt
Entry: U3AJ86_9RHOB
LinkDB: U3AJ86_9RHOB
Original site: U3AJ86_9RHOB 
ID   U3AJ86_9RHOB            Unreviewed;       406 AA.
AC   U3AJ86;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN   ORFNames=MBELCI_0890 {ECO:0000313|EMBL:GAD54838.1};
OS   Limimaricola cinnabarinus LL-001.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Limimaricola.
OX   NCBI_TaxID=1337093 {ECO:0000313|EMBL:GAD54838.1, ECO:0000313|Proteomes:UP000016566};
RN   [1] {ECO:0000313|EMBL:GAD54838.1, ECO:0000313|Proteomes:UP000016566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL-001 {ECO:0000313|EMBL:GAD54838.1,
RC   ECO:0000313|Proteomes:UP000016566};
RA   Nishi S., Tsubouchi T., Takaki Y., Koyanagi R., Satoh N., Maruyama T.,
RA   Hatada Y.;
RT   "Draft Genome Sequence of Loktanella cinnabarina LL-001T, Isolated from
RT   Deep-Sea Floor Sediment.";
RL   Genome Announc. 1:e00927-13(2013).
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC       from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC       produce L-alanine. {ECO:0000256|RuleBase:RU004506}.
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         ECO:0000256|RuleBase:RU004506};
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. Csd subfamily. {ECO:0000256|ARBA:ARBA00010447,
CC       ECO:0000256|RuleBase:RU004506}.
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:GAD54838.1}.
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DR   EMBL; BATB01000007; GAD54838.1; -; Genomic_DNA.
DR   RefSeq; WP_021692946.1; NZ_BATB01000007.1.
DR   AlphaFoldDB; U3AJ86; -.
DR   STRING; 1337093.MBELCI_0890; -.
DR   eggNOG; COG0520; Bacteria.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000016566; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004506};
KW   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          24..394
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   406 AA;  44134 MW;  0535BDBAC3249862 CRC64;
     MYDVEEIRAQ FPILSREING VPLVYLDNGA SAQKPQVVID AINRGYAQEY SNVHRGLHTL
     STISTERYEG TRDVVRKFLN AASAEEIILN TGTTEGINMV AYGWAMPRME PGDEIVLSIM
     EHHANIVPWH FLRERQGVVI KWVDVDANGD LDPQAVIDAI GPKTKLVAVT HMSNVLGTVV
     DVKAICDGAR ARGVPVLVDG SQAAVHMPVD VQAIGCDFYA ITGHKLYGPS GAGAIYVRSE
     RMAEMRPFMG GGDMIDRVTR DTVTYNEPPM RFEAGTPSIV STIGMGVALD WMMGVGMDDI
     AAHERHLRNR AIERFKGLNW LNVQGNSAGK GAIFSLTIEG GAHAHDISTV LDKKGIAVRA
     GTHCAMPLMD HLGVGATCRA SFGLYNTEAE VDRLVDALEL CHELFG
//
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