ID C6WDC5_ACTMD Unreviewed; 452 AA.
AC C6WDC5;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=Amir_5748 {ECO:0000313|EMBL:ACU39562.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU39562.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU39562.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
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; CP001630; ACU39562.1; -; Genomic_DNA.
DR RefSeq; WP_015804447.1; NC_013093.1.
DR AlphaFoldDB; C6WDC5; -.
DR SMR; C6WDC5; -.
DR STRING; 446462.Amir_5748; -.
DR KEGG; ami:Amir_5748; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_0_11; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000002213; Chromosome.
DR GO; GO:0008483; F:transaminase 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 Aminotransferase {ECO:0000313|EMBL:ACU39562.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW Transferase {ECO:0000313|EMBL:ACU39562.1}.
FT DOMAIN 48..415
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 452 AA; 47743 MW; 8FD99BED7B128D39 CRC64;
MTLAVSRTAA RTVVETADAA PVAAALPAVV GAALRVPLVT GERVEYANLD NAASTPCLEQ
VRDAVDELLP WYASVHRGAG FASKVSTRVY EQARDSVRRF TGARSSDTVV FTRNTTDSLN
ALARAVPRGT SVLLFDTEHH AALLPWRGPN VRRLRTPGTP AEAARVLDAA LAECPVGPRL
VVLTGASNVT GEVWPVAELA AIARRRGART VLDAAQLAPH RPLDIKELGV DYVAFSGHKL
YAPFGAGVLV GRADWLQAAE PYLVGGGATS LVTDHGDHLG VAWSRVPERH EAGSPNVVGV
HALAVACDVL GRNWNRAVAH ERALLERLRA GLATVPGVRE LSLFGSGQDR VGVVSFTVSG
QDSGYLAAAL SAEHGIGVRD GAFCAHVAVH RLTGGERALR ASLGLGSTEE HVDRLVAALR
SLITEGPKVA YAQRDGRWEP VVDDRALPPF LA
//
