ID L1P3N0_9FLAO Unreviewed; 382 AA.
AC L1P3N0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=HMPREF9075_01162 {ECO:0000313|EMBL:EKY10236.1};
OS Capnocytophaga sp. oral taxon 332 str. F0381.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1127692 {ECO:0000313|EMBL:EKY10236.1, ECO:0000313|Proteomes:UP000010419};
RN [1] {ECO:0000313|EMBL:EKY10236.1, ECO:0000313|Proteomes:UP000010419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0381 {ECO:0000313|EMBL:EKY10236.1,
RC ECO:0000313|Proteomes:UP000010419};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-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. 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:EKY10236.1}.
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DR EMBL; AMET01000082; EKY10236.1; -; Genomic_DNA.
DR RefSeq; WP_009415886.1; NZ_KB291317.1.
DR AlphaFoldDB; L1P3N0; -.
DR STRING; 1127692.HMPREF9075_01162; -.
DR PATRIC; fig|1127692.3.peg.1056; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_10; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000010419; 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:UP000010419}.
FT DOMAIN 3..372
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 382 AA; 42136 MW; CBA3D5EC5B869D5A CRC64;
MNIYFDNAAT TALHREVVAK MTEVLTDNYG NPSATYALGR KTRTLIETAR KQIAQQLGAQ
SSEIIFTSGG SEADNLILRG CVRDLGVRVI ITSLIEHHAV LHTVEALAKE YGIQIEYVHL
TAEGDVCLQH LETLLQQYAD QKVLVSLMHV NNEIGNILPL ATVAAFCKKY GAYFHSDTVQ
SVAHLPIDLR GVPVDFITAS AHKFHGPKGV GFAFIRKGIV LHPLIYGGEQ EKGLRAGTEA
VHNIVGMQEA LKLAYRDRAS HTEKLQQLKQ YFIAALKEHF PEVVFNGNSQ DKEKSSHTIL
NVGFPNWENK KDTLLFELDL KGVACSKGSA CQSGSVGESH VLQAFLPAES LRYPSLRFSF
SIQNTTEEVD NLIKILGEIA KK
//