TTCA_ACAM1
ID TTCA_ACAM1 Reviewed; 283 AA.
AC B0CEK4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=AM1_1954;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW26970.1; -; Genomic_DNA.
DR AlphaFoldDB; B0CEK4; -.
DR SMR; B0CEK4; -.
DR STRING; 329726.AM1_1954; -.
DR EnsemblBacteria; ABW26970; ABW26970; AM1_1954.
DR KEGG; amr:AM1_1954; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_026481_0_0_3; -.
DR OMA; MNLDQKQ; -.
DR Proteomes; UP000000268; Chromosome.
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; Reference proteome; RNA-binding;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..283
FT /note="tRNA-cytidine(32) 2-sulfurtransferase"
FT /id="PRO_0000348644"
FT MOTIF 49..54
FT /note="PP-loop motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT BINDING 127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
SQ SEQUENCE 283 AA; 32233 MW; 9BE1F3A76EF18F10 CRC64;
MSNLFMTATQ LHPSKQLKKL QARLRGLVGK AIRDYNLIEA GDRIMVCLSG GKDSYTLLDI
LLHLQRAAPI DFEILAVNLD QKQPNFPEQV LPNYLNQLQV PYRIVEEDTY STVKRVIPEG
KTMCGLCSRL RRGILYRVAQ EEQATKIALG HHREDIIETL FLNLFHAGKL EAMPPKLLSD
NRQHMVIRPL AYCPEADIQR YADLRQFPII PCTLCGSQET LQRVQVKQML QAWEQETPGR
LETIFRSLQN IELSQLADPQ LFDFAHLAIA ATPYADSPDR SGL
