ID A0A417HLX1_9FIRM Unreviewed; 445 AA.
AC A0A417HLX1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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 ECO:0000313|EMBL:RHT72826.1};
GN ORFNames=DW741_04625 {ECO:0000313|EMBL:RHT72826.1};
OS Ruminococcaceae bacterium AM28-23LB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=2292269 {ECO:0000313|EMBL:RHT72826.1, ECO:0000313|Proteomes:UP000284026};
RN [1] {ECO:0000313|EMBL:RHT72826.1, ECO:0000313|Proteomes:UP000284026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM28-23LB {ECO:0000313|EMBL:RHT72826.1,
RC ECO:0000313|Proteomes:UP000284026};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHT72826.1}.
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DR EMBL; QUJM01000007; RHT72826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417HLX1; -.
DR OrthoDB; 9765625at2; -.
DR Proteomes; UP000284026; Unassembled WGS sequence.
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; 3.30.70.1380; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01074};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01074};
KW Reference proteome {ECO:0000313|Proteomes:UP000284026}.
FT REGION 66..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 49311 MW; 6C80B9AED79D7B80 CRC64;
MKTLYLDCGM GAAGDMLAAA LLELVPQKED FLRRFAALGI PGVEAKVEPS VKCGITGTHF
SVSVHGQEET SQDVHDHEHD HDHEHSHDHE HSHDHEHGHD HEHGHDHEHS HDHEHSHDHE
HGHSHEHGHG HHHHSGMADI AHIVGHLDVP EKVKEDVLAV YGLIAQAESR AHGVPVEQIH
FHEVGSLDAV ADITAVCMLM AELAPEQVVA SPVHVGSGKV RCAHGVLPVP APATAYILED
VPIYGGKIQG ELCTPTGAAL LKHFATRFGD MPVMRIRKVG YGMGKKDFEA ANCVRVLWGE
TQEEAGQIVE LSCNMDDMTG EEMGFAMDRL FEAGALDVYT LPISMKKSRP GILLRVMCRP
EDREKMVEQI FHHTTTLGVR ESRMGRYTLK RQMEQVETPW GTIGEKTAQG YGTERSKYEY
EDLAALAIRE GVSLRQARAM VEKKK
//
