ID A0A167CHT3_9BACL Unreviewed; 383 AA.
AC A0A167CHT3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=PNBC_14060 {ECO:0000313|EMBL:OAB73214.1};
OS Paenibacillus crassostreae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1763538 {ECO:0000313|EMBL:OAB73214.1, ECO:0000313|Proteomes:UP000077134};
RN [1] {ECO:0000313|EMBL:OAB73214.1, ECO:0000313|Proteomes:UP000077134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0068 {ECO:0000313|EMBL:OAB73214.1,
RC ECO:0000313|Proteomes:UP000077134};
RA Shin S.-K., Yi H.;
RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL Submitted (FEB-2016) 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. 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:OAB73214.1}.
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DR EMBL; LSFN01000025; OAB73214.1; -; Genomic_DNA.
DR RefSeq; WP_068659176.1; NZ_LSFN01000025.1.
DR AlphaFoldDB; A0A167CHT3; -.
DR STRING; 1763538.LPB68_06230; -.
DR KEGG; pcx:LPB68_06230; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000077134; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077134}.
FT DOMAIN 4..367
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 383 AA; 42112 MW; 907393AC2903EC07 CRC64;
MNPIYLDHAA STPIHPEVAQ IMMKIMMEQY GNASSVHSFG RGAKRSLNGA RDRASRLLGC
YPDELVFTSG GTESDNLALF GVSSLLSHKG RHIITSSIEH HAILHSCSEL ERQGFQVTYL
PVDSTGQIRI EDVEKAMTDE TILISIMYGN NEVGTIQPIE EIGKLAQSRG ILFHVDAVQA
LETLPISCRD LPVDLMSFSA HKINGPQGVG ALYVRRSIQL NAQSYGGLQE KKRRAGTENI
AGVEGFAKAI ELIHEQIQER REYYLQLRTT MIATLEQVIG DDSFIVNGHP TQFLPHILNI
SIPEVDTETL LMSLDMEGIA ASSGSACTSG SLELSHVLEA MKLSDSIMRS AIRFSFGLGN
TTKEIEHVAQ IIGTILRRVR NRT
//