LARC_DESHD
ID LARC_DESHD Reviewed; 402 AA.
AC B8G2K7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=Dhaf_3339;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL21357.1; -; Genomic_DNA.
DR RefSeq; WP_015944549.1; NC_011830.1.
DR AlphaFoldDB; B8G2K7; -.
DR SMR; B8G2K7; -.
DR EnsemblBacteria; ACL21357; ACL21357; Dhaf_3339.
DR KEGG; dhd:Dhaf_3339; -.
DR HOGENOM; CLU_028523_2_1_9; -.
DR OMA; EILCKHE; -.
DR Proteomes; UP000007726; 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_1000149768"
SQ SEQUENCE 402 AA; 44761 MW; 98ABCD04EAC2340B CRC64;
MKAAYLDCFS GISGDMLLGA LVDAGLDFNL LQRDLAGLDL DEYELYEQKV LKQGIRGTQI
HVHALEGHVH RHLSDIQAII GRSALPPQVK EKSLEIFTRL GKAEAKIHGT DIEQIHFHEV
GAVDAIVDIV GAVIGFWRLG IEKVFASPIH VGKGFVKAAH GLLPVPAPAT LELLTGVPIY
AQDVEGELAT PTGAAIVTAY CREFGPFPKI RVERVGYGAG VKDLTIPNLL RLTVGELADE
DKGQEGIREG EALTLEVNID DMNPECYDYL FEKLFQAGAM DVYIQTIQMK KNRPAVLLTV
QTPYHKLEEM RKILFQETTT IGLRVYPIKK YMLPYELFTV ETNYGSAKVK VAFMEGRACT
VSPEYEDCRR LARLTGEPLK QIYEEIKEKA KILLYSTKYP ID