P152_METTH
ID P152_METTH Reviewed; 186 AA.
AC O26255;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein MTH_152;
GN OrderedLocusNames=MTH_152;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11017201; DOI=10.1038/82823;
RA Christendat D., Yee A., Dharamsi A., Kluger Y., Savchenko A., Cort J.R.,
RA Booth V., Mackereth C.D., Saridakis V., Ekiel I., Kozlov G., Maxwell K.L.,
RA Wu N., McIntosh L.P., Gehring K., Kennedy M.A., Davidson A.R., Pai E.F.,
RA Gerstein M., Edwards A.M., Arrowsmith C.H.;
RT "Structural proteomics of an archaeon.";
RL Nat. Struct. Biol. 7:903-909(2000).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the flavoredoxin family. {ECO:0000305}.
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DR EMBL; AE000666; AAB84658.1; -; Genomic_DNA.
DR PIR; G69069; G69069.
DR PDB; 1EJE; X-ray; 2.20 A; A=1-186.
DR PDBsum; 1EJE; -.
DR AlphaFoldDB; O26255; -.
DR SMR; O26255; -.
DR PRIDE; O26255; -.
DR EnsemblBacteria; AAB84658; AAB84658; MTH_152.
DR KEGG; mth:MTH_152; -.
DR PATRIC; fig|187420.15.peg.124; -.
DR HOGENOM; CLU_059021_3_1_2; -.
DR OMA; APFSCFT; -.
DR EvolutionaryTrace; O26255; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; Reference proteome.
FT CHAIN 1..186
FT /note="Protein MTH_152"
FT /id="PRO_0000085528"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:1EJE"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1EJE"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1EJE"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1EJE"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1EJE"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1EJE"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 122..135
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 138..150
FT /evidence="ECO:0007829|PDB:1EJE"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1EJE"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:1EJE"
SQ SEQUENCE 186 AA; 20323 MW; 6997E8C6D9234A89 CRC64;
MMSMDFEDFP VESAHRILTP RPTVMVTTVD EEGNINAAPF SFTMPVSIDP PVVAFASAPD
HHTARNIEST HEFVINITPA DIIERMWVTA RDIPAGENEL EAAGLAWTSS RRVKPPRIVE
APGHLECELL RMFEVGDHNL ITGSVVSASV RSGAVKEGLL DVESVKPVLH VGGNKFVVGD
HVRHVE