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Database: UniProt
Entry: E6KY61_9PAST
LinkDB: E6KY61_9PAST
Original site: E6KY61_9PAST 
ID   E6KY61_9PAST            Unreviewed;       408 AA.
AC   E6KY61;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   Name=iscS2 {ECO:0000313|EMBL:EFU67774.1};
GN   ORFNames=HMPREF9064_1093 {ECO:0000313|EMBL:EFU67774.1};
OS   Aggregatibacter segnis ATCC 33393.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=888057 {ECO:0000313|EMBL:EFU67774.1, ECO:0000313|Proteomes:UP000032871};
RN   [1] {ECO:0000313|EMBL:EFU67774.1, ECO:0000313|Proteomes:UP000032871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33393 {ECO:0000313|EMBL:EFU67774.1,
RC   ECO:0000313|Proteomes:UP000032871};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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. Csd subfamily.
CC       {ECO:0000256|ARBA:ARBA00010447}.
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:EFU67774.1}.
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DR   EMBL; AEPS01000005; EFU67774.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6KY61; -.
DR   STRING; 739.GCA_001059425_00751; -.
DR   HOGENOM; CLU_003433_2_3_6; -.
DR   Proteomes; UP000032871; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000032871};
KW   Transferase {ECO:0000313|EMBL:EFU67774.1}.
FT   DOMAIN          31..396
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   408 AA;  45352 MW;  FE842BBE7DFF2F69 CRC64;
     MASFQKVNYM NFDPMTFRQY FPYFTHNDAV VYLDNAATTL KPQCLIDATV DFYQSAGSVH
     RSQYDEKQTA LYEQARTRVK HLINAEDEQA VIWTSGTTQG INTVANGLLP HLKTGDEIII
     SEADHHANFV TWHQIAEKSG AKLHVLPIDD SWLINTETLL KQLNPNTKLV ALNFASNVTG
     TQQPVIQLIQ HIRDKSSAFI LLDAAQAISH VKIDLAELDV DFIAFSAHKI YGPTGLGVLS
     GKLSSLNLLQ PLQYGGKMIS KVSKEQITFS GLPYRLEAGT PNIAAVIGFN AVLAWLSQWD
     IAEMESSAVH LAEITRRRLS HYEKCKLFNS PQPSSVVSFV FEDINASDLA TLLAEQQIAL
     RVGEHCAQPY LARLGQTATL RLSFAPYNVA SEVETFFNAL DKSLELLR
//
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