LARC_THESQ
ID LARC_THESQ Reviewed; 402 AA.
AC B1L8M5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel insertion protein {ECO:0000255|HAMAP-Rule:MF_01074};
DE Short=P2TMN nickel insertion protein {ECO:0000255|HAMAP-Rule:MF_01074};
DE EC=4.99.1.12 {ECO:0000255|HAMAP-Rule:MF_01074};
DE AltName: Full=Nickel-pincer cofactor biosynthesis protein LarC {ECO:0000255|HAMAP-Rule:MF_01074};
GN Name=larC {ECO:0000255|HAMAP-Rule:MF_01074}; OrderedLocusNames=TRQ2_1826;
OS Thermotoga sp. (strain RQ2).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC unclassified Thermotoga.
OX NCBI_TaxID=126740;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RQ2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga sp. RQ2.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of a nickel-pincer cofactor
CC ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel
CC delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide
CC (P2TMN), to form the mature cofactor. Is thus probably required for the
CC activation of nickel-pincer cofactor-dependent enzymes.
CC {ECO:0000255|HAMAP-Rule:MF_01074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide =
CC Ni(2+) + pyridinium-3,5-bisthiocarboxylate mononucleotide;
CC Xref=Rhea:RHEA:54784, ChEBI:CHEBI:49786, ChEBI:CHEBI:137372,
CC ChEBI:CHEBI:137373; EC=4.99.1.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01074};
CC -!- SIMILARITY: Belongs to the LarC family. {ECO:0000255|HAMAP-
CC Rule:MF_01074}.
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DR EMBL; CP000969; ACB10154.1; -; Genomic_DNA.
DR RefSeq; WP_012311366.1; NC_010483.1.
DR AlphaFoldDB; B1L8M5; -.
DR SMR; B1L8M5; -.
DR EnsemblBacteria; ACB10154; ACB10154; TRQ2_1826.
DR KEGG; trq:TRQ2_1826; -.
DR HOGENOM; CLU_028523_2_1_0; -.
DR OMA; TCLGLDW; -.
DR OrthoDB; 1547060at2; -.
DR Proteomes; UP000001687; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051604; P:protein maturation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01074; LarC; 1.
DR InterPro; IPR002822; Ni_insertion.
DR PANTHER; PTHR36566; PTHR36566; 1.
DR Pfam; PF01969; DUF111; 1.
DR TIGRFAMs; TIGR00299; TIGR00299; 1.
PE 3: Inferred from homology;
KW Lyase; Nickel.
FT CHAIN 1..402
FT /note="Pyridinium-3,5-bisthiocarboxylic acid mononucleotide
FT nickel insertion protein"
FT /id="PRO_1000136697"
SQ SEQUENCE 402 AA; 44859 MW; 10A4E340EAF519A0 CRC64;
MRILYLDPFS GISGDMFLGL LVDLGVDPEK IKSRLEKLNV EFEFVVKKEN KKGVTATKVD
VVFPGKEHHE DHIVSDHDHH HHHGRHLSEI VEVLSRLEDP LKEKAIRMFE TLAEAESKIH
GLSKEKVHFH EVGAMDAVIE IAGAVAGLEL LGVEKVFCGT VNTGSGFVMT EHGRYPVPAP
ATAELLKGIP IYVDQKVRTE LVTPTGAVIL KSLVDEFRTP ILRVEKVGYG AGTMDLEIPN
VLRGYLGYIE PSERTGDVLI ETNVDDMSPQ LFGHLMERLF EAGAKDVFFT PIYMKKNRPA
VKVSVLCHES KKDEILKLLF KESTSIGARV FYPEKVEATR TVKTVKTEYG EIPVKIASFD
SEIVNISPEY EACKKIAQEK GIPLKEVYRA VCKSVSEVRD DV