ID F8ABU2_THEID Unreviewed; 776 AA.
AC F8ABU2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Cysteine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00041};
DE EC=6.1.1.16 {ECO:0000256|HAMAP-Rule:MF_00041};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041};
DE Short=CysRS {ECO:0000256|HAMAP-Rule:MF_00041};
GN Name=cysS {ECO:0000256|HAMAP-Rule:MF_00041};
GN OrderedLocusNames=Thein_0670 {ECO:0000313|EMBL:AEH44550.1};
OS Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfatatoraceae; Thermodesulfatator.
OX NCBI_TaxID=667014 {ECO:0000313|EMBL:AEH44550.1, ECO:0000313|Proteomes:UP000006793};
RN [1] {ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders L.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermodesulfatator indicus DSM 15286.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEH44550.1, ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RX PubMed=22768359; DOI=10.4056/sigs.2665915;
RA Anderson I., Saunders E., Lapidus A., Nolan M., Lucas S., Tice H.,
RA Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Chang Y.J.,
RA Brambilla E.M., Rohde M., Spring S., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of the thermophilic sulfate-reducing ocean
RT bacterium Thermodesulfatator indicus type strain (CIR29812(T)).";
RL Stand. Genomic Sci. 6:155-164(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00041};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00041};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00041};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR605856-50};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_00041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00041}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00041}.
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DR EMBL; CP002683; AEH44550.1; -; Genomic_DNA.
DR RefSeq; WP_013907295.1; NC_015681.1.
DR AlphaFoldDB; F8ABU2; -.
DR STRING; 667014.Thein_0670; -.
DR PaxDb; 667014-Thein_0670; -.
DR KEGG; tid:Thein_0670; -.
DR PATRIC; fig|667014.3.peg.694; -.
DR eggNOG; COG0031; Bacteria.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_5_0_0; -.
DR InParanoid; F8ABU2; -.
DR OrthoDB; 9815130at2; -.
DR Proteomes; UP000006793; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:InterPro.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd01561; CBS_like; 1.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR005856; Cys_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01136; cysKM; 1.
DR NCBIfam; TIGR00435; cysS; 1.
DR PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09190; DALR_2; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SMART; SM00840; DALR_2; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00041};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00041}; Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00041};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR605856-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000006793};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT DOMAIN 660..721
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|SMART:SM00840"
FT BINDING 76
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 181..185
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 262
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 545
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 549
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT MOD_RES 46
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 776 AA; 87474 MW; E047F3F6042070ED CRC64;
MARKKYGNIL DRIGNTPLVP IRRLRSNPKV QIYGKIEAVN PGGSVKDRIA LSMIEAAEES
GELTREKIII EASSGNTGIG LALVSAVKGY RCLIAMSEAA SIERRKIMRA FGAEILLTSA
EKGTDGAIEA VYELARKYPD KYYLTDQFNN PANWQAHYYG TAPEIWRDTE GKVTHIVAGM
GTTGTLMGLA RFFRDKNLPA KVIGVEPLPG HRLQGLKNMK ESYPPGIFDK KILAEIINVP
DEEAFELTRR LAREEGIFVG MSSGAALYGA LELAKRIDEG VIVVIFPDGG ERYLSTSLWD
FEDLPKQGPR FTNTLTRKTE AFKPLKEGLV GIYTCGPTVH RRPHLGLYRR MITADLLRRY
LEYKGYEVTH VVNLTDFDDK TIQAALENKI PLKELTQRVA HEFFEDLKTL NISQASFYPR
ASEHIEEMIE LTRRLIEKDF AYVRHGSVYF DVSKLKNYGL LSKIDLTKLK TGATVDLEDY
EKDDPLDFTL FKRASLQELK EGFYVETEWG KVRPGWHIQC AAMSLKYLGE EFDIHTSGTD
LIFPHHEDEI AIARALTGKI PARFWLHSAL VSRKGKKMSF SAGNAITIPE LLAKGYSGRG
IRYFLLRTHY RKPLDFSFKA LDEAAKALKG LDLFMVFLAR EPSGQTDFPV AQTVENFLEC
FEAALDDDLN ISKAFAALFE FTNRLEPVLS REGLDEDDTL KVKEALSKVN KVLAIIREAK
IAAEPEVKEV LARREEARQK GLFEKADRLR EELIKQGFWV IDTPRGPIAA AFDHEA
//
