ID F7S405_9PROT Unreviewed; 414 AA.
AC F7S405;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-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 ORFNames=APM_1056 {ECO:0000313|EMBL:EGO96132.1};
OS Acidiphilium sp. PM.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=1043206 {ECO:0000313|EMBL:EGO96132.1, ECO:0000313|Proteomes:UP000004823};
RN [1] {ECO:0000313|EMBL:EGO96132.1, ECO:0000313|Proteomes:UP000004823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM {ECO:0000313|EMBL:EGO96132.1,
RC ECO:0000313|Proteomes:UP000004823};
RX PubMed=21914891; DOI=10.1128/JB.05386-11;
RA San Martin-Uriz P., Gomez M.J., Arcas A., Bargiela R., Amils R.;
RT "Draft Genome Sequence of the Electricigen Acidiphilium sp. Strain PM (DSM
RT 24941).";
RL J. Bacteriol. 193:5585-5586(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. 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:EGO96132.1}.
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DR EMBL; AFPR01000098; EGO96132.1; -; Genomic_DNA.
DR RefSeq; WP_007422210.1; NZ_AFPR01000098.1.
DR AlphaFoldDB; F7S405; -.
DR HOGENOM; CLU_003433_2_5_5; -.
DR Proteomes; UP000004823; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EGO96132.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000313|EMBL:EGO96132.1}.
FT DOMAIN 32..401
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 414 AA; 44774 MW; CD80B46478E78B74 CRC64;
MSAAIEQPGF DIARIRADFP ILSQTVHGKK LVFLDSGASA QKPRAVIDAM VRSMETRYAN
VHRGLHWLSE RASDDYEAAR DKVAAFLNAA REEIVFVRNA TEGINLVAAT FGRSALRPGD
AVVVSEMEHH ANLVPWQMLR DSHVIELRIA KITDAGELDF ADLERQFADG RVRLLAITHM
SNVLGTYTPV ERLAAFAHER GARLLLDGAQ AVVHRAVDVR AIDADFYVFS GHKLYGPSGI
GVLFGKRELL DAMPPFLGGG DMIRSVSYEK STWAEPPYRF EAGTPAIVEA VGLAAAIDYV
NAIGFPAIAS HERALTDHAL ATLDAIGGVH VVGRAQDRGG VVAFTMDGVH AHDVATLLDK
QGIAVRAGHH CAEPLTRRLG LDSTARATFG VYTTMEEIDA LAAGLRRVQQ VFGG
//
