ID   Y1914_METTH             Reviewed;         377 AA.
AC   O27936;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=UPF0425 pyridoxal phosphate-dependent protein MTH_1914;
GN   OrderedLocusNames=MTH_1914;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the UPF0425 family. {ECO:0000305}.
CC   -!- CAUTION: Despite a certain similarity to selA, this is not selA (see AC
CC       Q57622). {ECO:0000305}.
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DR   EMBL; AE000666; AAB86374.1; -; Genomic_DNA.
DR   PIR; F69122; F69122.
DR   RefSeq; WP_010877510.1; NC_000916.1.
DR   AlphaFoldDB; O27936; -.
DR   SMR; O27936; -.
DR   STRING; 187420.MTH_1914; -.
DR   EnsemblBacteria; AAB86374; AAB86374; MTH_1914.
DR   GeneID; 1470999; -.
DR   KEGG; mth:MTH_1914; -.
DR   PATRIC; fig|187420.15.peg.1870; -.
DR   HOGENOM; CLU_055443_0_0_2; -.
DR   OMA; RIDFCSK; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR020033; PyrdxlP-dep_transferase_arc.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR018319; SelA-like.
DR   Pfam; PF03841; SelA; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03576; pyridox_MJ0158; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..377
FT                   /note="UPF0425 pyridoxal phosphate-dependent protein
FT                   MTH_1914"
FT                   /id="PRO_0000285290"
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   377 AA;  41074 MW;  8DBDBBB60BAC4FD0 CRC64;
     MLEDPVNEVK RREHALRIIG EKMKKHGRDG IYDLTGLSGG FPLEEEDLDL IETYVGPAIF
     EEKLQEAGRE HMGGEMIAAF NRTSSAILAA VLALTEPGST VFHYLPELPS HPSVPGSTEL
     ASAGYQETED FTEKPPADTS LVVVTGSTMD HRVVGESDLV RVIEIAHDAG IPVLVDDASG
     ARLRTVLYGQ RRACDLGADL AVTSTDKLMH GPRGGLMAGR AELIERVKSK AYQFGLEAQP
     PLVAAMVRAL EEFEPSEIRD AIKRKEEFLR DFRGPEVEET PTGFIIKSSS LEDLQGSGYD
     GDEISTALSM ILLSEHGIVT IPAVGMPGAS KTLRFDLAAR DAGRIEISFL REAIYDAIKL
     VSGFINDDEK MRRLILG