ID Q2FRS4_METHJ Unreviewed; 235 AA.
AC Q2FRS4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN OrderedLocusNames=Mhun_3068 {ECO:0000313|EMBL:ABD42755.1};
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD42755.1, ECO:0000313|Proteomes:UP000001941};
RN [1] {ECO:0000313|Proteomes:UP000001941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC {ECO:0000313|Proteomes:UP000001941};
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|RuleBase:RU004168}.
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DR EMBL; CP000254; ABD42755.1; -; Genomic_DNA.
DR RefSeq; WP_011450006.1; NC_007796.1.
DR AlphaFoldDB; Q2FRS4; -.
DR STRING; 323259.Mhun_3068; -.
DR EnsemblBacteria; ABD42755; ABD42755; Mhun_3068.
DR GeneID; 3922764; -.
DR KEGG; mhu:Mhun_3068; -.
DR eggNOG; arCOG01674; Archaea.
DR HOGENOM; CLU_080336_0_0_2; -.
DR InParanoid; Q2FRS4; -.
DR OrthoDB; 378895at2157; -.
DR Proteomes; UP000001941; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.100; -; 1.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR47268; ACYLPHOSPHATASE; 1.
DR PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Reference proteome {ECO:0000313|Proteomes:UP000001941}.
FT DOMAIN 3..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 130..192
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 235 AA; 27653 MW; 4975F070DCA8B4D5 CRC64;
MKRLIITAIG EVQRVGYRDR VTKIARKNNI TGIVRNCPGY DVEIIAEGNE VDLDRFISQI
KIHEDPIYVE SIKIDKGTYE GKWEYFEIQR GKPDEELGER LDAALTYLVR IDSNSRRSVE
IGEQMLVKQD QMLDKQDQML DKQDQMLDKQ DQMLDKQDQM LDKQDQMLDK QDQMLDKQDQ
MLANQNYQIS LQKITNQEIQ EMRSDIKDSL NTKYQFIEQQ LHEIQTVLKN AGMMS
//
