ID Q031J4_LACLS Unreviewed; 381 AA.
AC Q031J4;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Cysteine sulfinate desulfinase/cysteine desulfurase related enzyme {ECO:0000313|EMBL:ABJ72128.1};
GN OrderedLocusNames=LACR_0534 {ECO:0000313|EMBL:ABJ72128.1};
OS Lactococcus lactis subsp. cremoris (strain SK11).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=272622 {ECO:0000313|EMBL:ABJ72128.1, ECO:0000313|Proteomes:UP000000240};
RN [1] {ECO:0000313|EMBL:ABJ72128.1, ECO:0000313|Proteomes:UP000000240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK11 {ECO:0000313|EMBL:ABJ72128.1,
RC ECO:0000313|Proteomes:UP000000240};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
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DR EMBL; CP000425; ABJ72128.1; -; Genomic_DNA.
DR RefSeq; WP_011675547.1; NC_008527.1.
DR AlphaFoldDB; Q031J4; -.
DR KEGG; llc:LACR_0534; -.
DR HOGENOM; CLU_003433_0_0_9; -.
DR Proteomes; UP000000240; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF50; CYSTEINE DESULFURASE ISCS 2-RELATED; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 2..365
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 381 AA; 41891 MW; 228A056D1999C320 CRC64;
MIYFDNSATT AVNPMVLRTY TDVATKIMGN PSSLHGLGTT ATRLLEASRR QIAELLGLDS
QEIFFTSGGT EGDNWIIKGV AFEKRPYGNH IIVSSVEHPA VKNAAEWLKT QGFELDYAPV
DADGFVIVSE LEKLIRDETI LISVMAVNNE VGAIQPIQEI SELLADKPTI SFHVDAVQAI
GKVPLETWLT DRLDFATLSA HKFHGPRGVG IVVAKKGKRL TPLLHGGGQE HNWRSTTENL
AGIAATSKAL RLAVDEDDFK RKKMLAMKQA ILEELEKYKK VYVFSKMTDF APNILTFGIR
GVRGEVVVHA FEQHDIYIST TSACSSKKNA ADGTLVAMNV PSKLATSAVR ISLDPTNNMA
EVEQFLTVFR QIYQELEKVS G
//
