ID A0A1H8PUT2_9BURK Unreviewed; 319 AA.
AC A0A1H8PUT2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=tRNA-cytidine(32) 2-sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_01850};
DE EC=2.8.1.- {ECO:0000256|HAMAP-Rule:MF_01850};
DE AltName: Full=Two-thiocytidine biosynthesis protein A {ECO:0000256|HAMAP-Rule:MF_01850};
DE AltName: Full=tRNA 2-thiocytidine biosynthesis protein TtcA {ECO:0000256|HAMAP-Rule:MF_01850};
GN Name=ttcA {ECO:0000256|HAMAP-Rule:MF_01850};
GN ORFNames=SAMN05428959_108107 {ECO:0000313|EMBL:SEO45531.1};
OS Duganella sp. CF517.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEO45531.1, ECO:0000313|Proteomes:UP000198691};
RN [1] {ECO:0000313|Proteomes:UP000198691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01850};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01850};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01850};
CC -!- PATHWAY: tRNA modification. {ECO:0000256|HAMAP-Rule:MF_01850}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01850}.
CC -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000256|HAMAP-
CC Rule:MF_01850}.
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DR EMBL; FODC01000008; SEO45531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8PUT2; -.
DR STRING; 1881038.SAMN05428959_108107; -.
DR OrthoDB; 9801054at2; -.
DR Proteomes; UP000198691; Unassembled WGS sequence.
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 CDD; cd01993; Alpha_ANH_like_II; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 PANTHER; PTHR43686; SULFURTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR43686:SF1; TRNA-CYTIDINE(32) 2-SULFURTRANSFERASE; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01850};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01850};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01850};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01850};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01850};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01850};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01850};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01850}; Reference proteome {ECO:0000313|Proteomes:UP000198691};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01850};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01850};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01850}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01850}.
FT DOMAIN 55..217
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 60..65
FT /note="PP-loop motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01850"
FT BINDING 135
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01850"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01850"
FT BINDING 226
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01850"
SQ SEQUENCE 319 AA; 35866 MW; 9303FA1CBCB5124C CRC64;
MNAPLHLPQQ DQAPAAAPER DPTDSRRFEL LQKKLRTQTG KAIVDFDMIT EGDLVMVCMS
GGKDSYAMLD ILMHLRKIAP VKFDLIAVNL DQKQPGFPEH VLPEYFQKIG VPYKIVEQDT
YSIVTEKIEP GKTTCSLCSR LRRGILYRTA KELGATKIAL GHHQGDILET FLLNMFYGGT
IKTMPARLTA DDGENVVIRP LAYCREQDIE KYAGKMGFPI IPCNLCGSQP NLQRQAMKEM
LATWQQKNPL WIKSMFTAMG NIKPSHMMDR GLFDFSKNEM REAEGAFTGD ILFDKDESIT
LDGVNGAFAI QSEVLKRAQ
//
