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Database: UniProt
Entry: M7PSQ7_9GAMM
LinkDB: M7PSQ7_9GAMM
Original site: M7PSQ7_9GAMM 
ID   M7PSQ7_9GAMM            Unreviewed;       407 AA.
AC   M7PSQ7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   05-DEC-2018, entry version 34.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|RuleBase:RU004506, ECO:0000256|SAAS:SAAS00369712};
DE            EC=2.8.1.7 {ECO:0000256|RuleBase:RU004506, ECO:0000256|SAAS:SAAS00369712};
GN   ORFNames=MPL1_05007 {ECO:0000313|EMBL:EMR13489.1};
OS   Methylophaga lonarensis MPL.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR13489.1, ECO:0000313|Proteomes:UP000012019};
RN   [1] {ECO:0000313|EMBL:EMR13489.1, ECO:0000313|Proteomes:UP000012019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MPL {ECO:0000313|EMBL:EMR13489.1,
RC   ECO:0000313|Proteomes:UP000012019};
RX   PubMed=23661481;
RA   Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P.,
RA   Murrell J.C., Shouche Y.S.;
RT   "Draft Genome Sequence of Methylophaga lonarensis MPLT, a
RT   Haloalkaliphilic (Non-Methane-Utilizing) Methylotroph.";
RL   Genome Announc. 1:E00202-13(2013).
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium
CC       atoms from L-cysteine, L-cystine, L-selenocysteine, and L-
CC       selenocystine to produce L-alanine.
CC       {ECO:0000256|RuleBase:RU004506}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH +
CC         L-alanine; Xref=Rhea:RHEA:43892, ChEBI:CHEBI:29917,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428,
CC         Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739; EC=2.8.1.7;
CC         Evidence={ECO:0000256|RuleBase:RU004506,
CC         ECO:0000256|SAAS:SAAS00369696};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU004504,
CC         ECO:0000256|SAAS:SAAS00608357};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily.
CC       {ECO:0000256|RuleBase:RU004506, ECO:0000256|SAAS:SAAS00544087}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EMR13489.1}.
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DR   EMBL; APHR01000022; EMR13489.1; -; Genomic_DNA.
DR   RefSeq; WP_009726013.1; NZ_APHR01000022.1.
DR   EnsemblBacteria; EMR13489; EMR13489; MPL1_05007.
DR   PATRIC; fig|1286106.3.peg.1008; -.
DR   OrthoDB; POG091H02CX; -.
DR   BioCyc; MLON1286106:G1HG4-984-MONOMER; -.
DR   Proteomes; UP000012019; 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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000012019};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004506,
KW   ECO:0000256|SAAS:SAAS00023586};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012019};
KW   Transferase {ECO:0000256|RuleBase:RU004506,
KW   ECO:0000256|SAAS:SAAS00446885}.
FT   DOMAIN       26    395       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   407 AA;  44647 MW;  342C29426BBCAD7A CRC64;
     MRAFDIEQIR ADFPILHQQI NGQPLVYLDN AASSQKPLQV IEAVDHYYRT DNANVHRGVH
     RLSQRATDAF EASRSTVRDY LNASSDREIV FVRGATEAIN LVAQSFVRPM IVEGDEILIS
     HLEHHANIVP WQMLCEQTGA QLKVIPMTDT GELDLTQIDE LLNSRTKILS IGHVSNALGT
     VNPVKMLTEK ARAKGIPVLI DGAQAVPHLQ VDVQALDCDF YVFSGHKLFA PTGIGVLYGR
     QQLLEAMPPY QGGGDMILSV SFSGTIYNEL PYKFEAGTPH IAGAIGLAAA IDYIQQFGME
     VLAAHEHHLL DLATAKLQAM DGVRIIGTAK EKASVLSFMI DGVHPHDVGT IFDQQGVAIR
     TGHHCAQPVM EYFDIPATAR ASFAFYNSEQ EVDALVAAIK KTQELFG
//
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