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TTCA_DECAR
ID   TTCA_DECAR              Reviewed;         287 AA.
AC   Q477W2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=tRNA-cytidine(32) 2-sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_01850};
DE            EC=2.8.1.- {ECO:0000255|HAMAP-Rule:MF_01850};
DE   AltName: Full=Two-thiocytidine biosynthesis protein A {ECO:0000255|HAMAP-Rule:MF_01850};
DE   AltName: Full=tRNA 2-thiocytidine biosynthesis protein TtcA {ECO:0000255|HAMAP-Rule:MF_01850};
GN   Name=ttcA {ECO:0000255|HAMAP-Rule:MF_01850}; OrderedLocusNames=Daro_4143;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
CC   -!- FUNCTION: Catalyzes the ATP-dependent 2-thiolation of cytidine in
CC       position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms
CC       are provided by the cysteine/cysteine desulfurase (IscS) system.
CC       {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-
CC         [cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP +
CC         diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase];
CC         Xref=Rhea:RHEA:57048, Rhea:RHEA-COMP:10288, Rhea:RHEA-COMP:12157,
CC         Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:14821, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963,
CC         ChEBI:CHEBI:82748, ChEBI:CHEBI:141453, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01850};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57049;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01850};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01850};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01850};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by
CC       three Cys residues, the fourth Fe has a free coordination site that may
CC       bind a sulfur atom transferred from the persulfide of IscS.
CC       {ECO:0000255|HAMAP-Rule:MF_01850};
CC   -!- PATHWAY: tRNA modification. {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- MISCELLANEOUS: The thiolation reaction likely consists of two steps: a
CC       first activation step by ATP to form an adenylated intermediate of the
CC       target base of tRNA, and a second nucleophilic substitution step of the
CC       sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S
CC       cluster. {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01850}.
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DR   EMBL; CP000089; AAZ48869.1; -; Genomic_DNA.
DR   RefSeq; WP_011289863.1; NC_007298.1.
DR   AlphaFoldDB; Q477W2; -.
DR   SMR; Q477W2; -.
DR   STRING; 159087.Daro_4143; -.
DR   EnsemblBacteria; AAZ48869; AAZ48869; Daro_4143.
DR   KEGG; dar:Daro_4143; -.
DR   eggNOG; COG0037; Bacteria.
DR   HOGENOM; CLU_026481_0_0_4; -.
DR   OMA; MNLDQKQ; -.
DR   OrthoDB; 1051352at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01850; TtcA; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012089; tRNA_Cyd_32_2_STrfase.
DR   InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   PIRSF; PIRSF004976; ATPase_YdaO; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Magnesium;
KW   Metal-binding; Nucleotide-binding; RNA-binding; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..287
FT                   /note="tRNA-cytidine(32) 2-sulfurtransferase"
FT                   /id="PRO_0000348708"
FT   MOTIF           39..44
FT                   /note="PP-loop motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   BINDING         114
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   BINDING         117
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   BINDING         205
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
SQ   SEQUENCE   287 AA;  32176 MW;  B61A6C4B3ADE1B2D CRC64;
     MTPSNTLQKL RKYLEGRTGK AIIDYNMIED GDTVLVCVSG GKDSYTLLAM LMALQQRAPV
     KFRLIAMNLD QKQPGFPADI LPRYFESIGI EYRIVEADTY SVVKEKIPEG KTTCSLCSRL
     RRGIIYRTAK ELGANKIALG HHRDDMVHTL FLNLLFGGKL KAMPPKLVTD DKSHVVIRPL
     AYCAEADIAK FARGMEFPII PCNLCGSQDN LQRQKIREMM QEWDKRYPGR TESVFTAMQN
     VVPSHLADAD LFDFRGLTLD TPVDEGDIAF DAPEMPISGM IPISQTA
 
 
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