ID A0A1Y4EQG5_9FIRM Unreviewed; 420 AA.
AC A0A1Y4EQG5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=B5F54_11925 {ECO:0000313|EMBL:OUO73315.1};
OS Anaeromassilibacillus sp. An250.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaeromassilibacillus.
OX NCBI_TaxID=1965604 {ECO:0000313|EMBL:OUO73315.1, ECO:0000313|Proteomes:UP000195568};
RN [1] {ECO:0000313|Proteomes:UP000195568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An250 {ECO:0000313|Proteomes:UP000195568};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO73315.1}.
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DR EMBL; NFJK01000013; OUO73315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4EQG5; -.
DR OrthoDB; 9765625at2; -.
DR Proteomes; UP000195568; 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; 3.10.20.300; 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|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:UP000195568}.
FT REGION 69..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 44482 MW; A820B2516DDD568E CRC64;
MRTLYIECNM GAAGDMLLAA LYELLEDKSA FLDTMNGLGL PGVHLEAVPG TTCGIAGTHM
RVTVHGEEEH EPAAGHGHGH AHGHDHAHPH EHAHAHAHHH ATPGHIAEII DGLTLPDAVK
QHARSVYDAI AVAEAKAHGC PVGDVHYHEV GALDAVADVT GVCYALHLLQ PERVVVSPIH
VGSGTVRCAH GVMPVPAPAT ANLLTGVPIY GGAVQGELCT PTGAVLLTHF AASFGPMPVM
SVEAAGVGIG TKTFEQANCV RAFLGETVDE TNGEIVELVC NIDDMTPEAL AFASARLLDL
GALDVYTVPG TMKKGRPGHV LTVLCRREQE GEMARQVLAQ TTTNGLRVRR CGKYFLTPGA
GEAATQWGPV RVKWARGFGV THCKPEYDDV ARLAREHGVP FQQVQTDAVR NLPAEGEETR
//
