ID L0KBY4_HALHC Unreviewed; 383 AA.
AC L0KBY4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=Halha_2184 {ECO:0000313|EMBL:AGB42065.1};
OS Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Halobacteroides.
OX NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB42065.1, ECO:0000313|Proteomes:UP000010880};
RN [1] {ECO:0000313|Proteomes:UP000010880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC {ECO:0000313|Proteomes:UP000010880};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Halobacteroides halobius DSM 5150.";
RL Submitted (FEB-2012) 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}.
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DR EMBL; CP003359; AGB42065.1; -; Genomic_DNA.
DR RefSeq; WP_015327779.1; NC_019978.1.
DR AlphaFoldDB; L0KBY4; -.
DR STRING; 748449.Halha_2184; -.
DR KEGG; hhl:Halha_2184; -.
DR PATRIC; fig|748449.3.peg.2098; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_4_9; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000010880; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
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; IPR010969; Cys_dSase-rel_unknwn_funct.
DR InterPro; IPR010970; Cys_dSase_SufS.
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 NCBIfam; TIGR01977; am_tr_V_EF2568; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF4; ISOPENICILLIN N EPIMERASE; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000010880}.
FT DOMAIN 2..370
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 383 AA; 42111 MW; 3DE33D03CCF30C65 CRC64;
MIYFDNAATT WQKPEIVYQT VDDVLRNKSG NPSRGSHQIA LEASRVIFKA RNKVANFFNI
PDSRQIVFTK NATEATNLVF KGLLEKGDHV IISSLEHNAI ARPLHRLEEE GIISLTVVDT
EEGKEAFLKN IEGIITDQTK LIAMTHASNV TGNILPIKEV GEIAKQQGVY FLTDVAQTAG
IVPLDVQELK VDFLIFTGHK GLFGPQGVGG LYLTSDIKFK PLLEGGTGGS SKERLNPDML
PDKYESGTLN TPGVAGLKAG IEFIEKTTLE EIKAQEEKLV EQLMIGLEKL EEVEILTSQM
GQDKVGVTSF RVKGVEPATI GHILNSKYDI AVRTGIHCAP LAHQSIGTYN TGTVRVSFSY
FNTLKEVEQL LKALQEIINS KDY
//
