ID A0A348AQF7_9FIRM Unreviewed; 411 AA.
AC A0A348AQF7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel insertion protein {ECO:0000256|HAMAP-Rule:MF_01074};
DE Short=P2TMN nickel insertion protein {ECO:0000256|HAMAP-Rule:MF_01074};
DE EC=4.99.1.12 {ECO:0000256|HAMAP-Rule:MF_01074};
DE AltName: Full=Nickel-pincer cofactor biosynthesis protein LarC {ECO:0000256|HAMAP-Rule:MF_01074};
GN Name=larC {ECO:0000256|HAMAP-Rule:MF_01074};
GN ORFNames=MAMMFC1_04017 {ECO:0000313|EMBL:BBB93305.1};
OS Methylomusa anaerophila.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Methylomusa.
OX NCBI_TaxID=1930071 {ECO:0000313|EMBL:BBB93305.1, ECO:0000313|Proteomes:UP000276437};
RN [1] {ECO:0000313|EMBL:BBB93305.1, ECO:0000313|Proteomes:UP000276437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMFC1 {ECO:0000313|EMBL:BBB93305.1,
RC ECO:0000313|Proteomes:UP000276437};
RX PubMed=29458677; DOI=10.1099/ijsem.0.002635;
RA Amano N., Yamamuro A., Miyahara M., Kouzuma A., Abe T., Watanabe K.;
RT "Methylomusa anaerophila gen. nov., sp. nov., an anaerobic methanol-
RT utilizing bacterium isolated from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 68:1118-1122(2018).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01074};
CC -!- SIMILARITY: Belongs to the LarC family. {ECO:0000256|HAMAP-
CC Rule:MF_01074}.
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DR EMBL; AP018449; BBB93305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348AQF7; -.
DR KEGG; mana:MAMMFC1_04017; -.
DR OrthoDB; 9765625at2; -.
DR Proteomes; UP000276437; 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 Gene3D; 3.10.20.300; mk0293 like domain; 1.
DR Gene3D; 3.30.70.1380; Transcriptional regulatory protein pf0864 domain like; 1.
DR HAMAP; MF_01074; LarC; 1.
DR InterPro; IPR002822; Ni_insertion.
DR NCBIfam; TIGR00299; nickel pincer cofactor biosynthesis protein LarC; 1.
DR PANTHER; PTHR36566; NICKEL INSERTION PROTEIN-RELATED; 1.
DR PANTHER; PTHR36566:SF1; NICKEL INSERTION PROTEIN-RELATED; 1.
DR Pfam; PF01969; Ni_insertion; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01074};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01074};
KW Reference proteome {ECO:0000313|Proteomes:UP000276437}.
SQ SEQUENCE 411 AA; 44407 MW; D7E8162739165D13 CRC64;
MNANGTAIKT KAAFCDCFAG ISGNMMLGAL IDIGLPEEKL KKELAKLPVH GYEIKTARVD
KCGISAVHVD VIVGQDQQHR HLSDILDIIE NSTLSDAVKE KSTSVFRRLA EAEAKVHGVA
LQEVHFHEVG AVDAIIDVVG TIWGLEYMGI EALYTSKLHV GSGFTECCHG TIPVPAPATV
ELLIGIPYYQ GDIKKELVTP TGAAIVASLG QGFGSMPEAF VSKKVGYGAG TWNLPIPNIL
RLYIGEIVGI DPNLEQYNKD EQAASGSVTV IEANIDDLNP QVYPFVLDKL LAAGALDAWI
TPIIMKKGRP AVKLSALVEG TNKTKAAEII LTETSSIGVR FYEAGRLVAD REFLPVITPW
GQVRVKISSY QGKIINVAPE YEDCRKLATE RGVPLKVVQH IALKEAMPFV R
//
