ID I4D7Z8_DESAJ Unreviewed; 438 AA.
AC I4D7Z8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=Desaci_3013 {ECO:0000313|EMBL:AFM41922.1};
OS Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM41922.1, ECO:0000313|Proteomes:UP000002892};
RN [1] {ECO:0000313|EMBL:AFM41922.1, ECO:0000313|Proteomes:UP000002892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22704 / JCM 16185 / SJ4
RC {ECO:0000313|Proteomes:UP000002892};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
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}.
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DR EMBL; CP003639; AFM41922.1; -; Genomic_DNA.
DR RefSeq; WP_014827915.1; NC_018068.1.
DR AlphaFoldDB; I4D7Z8; -.
DR STRING; 646529.Desaci_3013; -.
DR KEGG; dai:Desaci_3013; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_0_9; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000002892; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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 Lyase {ECO:0000313|EMBL:AFM41922.1}.
FT DOMAIN 32..422
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 438 AA; 49405 MW; C93A30E090B884AF CRC64;
MNYKLSESIY RHLVMGTDMK IPLGNGEWAT SINFDNAAST PPFVSVMEEI NRFAPMYSSV
HRGTGYKSRY SSQLYEEARS EVLNFVNADP VNDTVIFVKN TTEAINKLSY RLWEDNKKSI
VLSTWMEHHS NDLPWRNKFQ VDYVEVNSQG KLNLTDLEHK LMRYKGKVKL VTVTGASNVT
GYINPIHKIA ELAHQYRAKI LVDGAQMVPH TLVNMRPQNP LQRIDYLAFS AHKMYAPFGS
GVLIGPRETF QKGVSEMVGG GTAEIVTHDW VIWNDPPHKD EAGSPNVMGV AALVAAIKTL
CALDMRKIDH YEYQLAEYAY SGLKSIPGIT LYTQYSPGEP HIGVIPFNVK GLHHERVASI
LSQEAGIAVR TGCFCTQPYI QKLLAISPKQ MEYYKKSRST SRPGVVRISF GLYNNFNEIN
NLLQTLEQIV RHPTMIIS
//
