ID A0A1H3YK49_9BURK Unreviewed; 318 AA.
AC A0A1H3YK49;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05421875_105140 {ECO:0000313|EMBL:SEA11332.1};
OS Acidovorax soli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=592050 {ECO:0000313|EMBL:SEA11332.1, ECO:0000313|Proteomes:UP000199002};
RN [1] {ECO:0000313|EMBL:SEA11332.1, ECO:0000313|Proteomes:UP000199002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25157 {ECO:0000313|EMBL:SEA11332.1,
RC ECO:0000313|Proteomes:UP000199002};
RA de Groot N.N.;
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; FNQJ01000005; SEA11332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3YK49; -.
DR STRING; 592050.SAMN05421875_105140; -.
DR Proteomes; UP000199002; 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};
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 60..224
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT MOTIF 66..71
FT /note="PP-loop motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01850"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01850"
FT BINDING 144
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01850"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01850"
SQ SEQUENCE 318 AA; 35617 MW; 81F4730D8747260B CRC64;
MNAIDSNAWT GEEAATAVAE PARAPADFKI ERETHKLEKR LCREVGKAIV HYNMIEEGDK
VMVCMSGGKD SYALLDILLK LKARAPIHFD LVAVNLDQKQ PGFPEHVLPD YLKSTGMPFH
IENEDTYSIV KRLIPEGKTT CSLCSRLRRG ILYRVADELG CTKIALGHHR DDILQTLLLN
MFFGGKMKSM PPKLVSDDGR HVVIRPLAFV AEKDTARWAQ HRNFPIIPCN LCGSQENLQR
KQVGEMLRDW EKRFPGRVEN MFNALQNVVP SHLLDGALYD FKGARATGVA DENGDKAFDA
EEFPAPSALP GLQVLRIQ
//
