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Database: UniProt/TrEMBL
Entry: Q2FP88_METHJ
LinkDB: Q2FP88_METHJ
Original site: Q2FP88_METHJ 
ID   Q2FP88_METHJ            Unreviewed;       302 AA.
AC   Q2FP88;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068};
DE            EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068};
GN   OrderedLocusNames=Mhun_1466 {ECO:0000313|EMBL:ABD41200.1};
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:ABD41200.1, 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   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family.
CC       {ECO:0000256|ARBA:ARBA00008116}.
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DR   EMBL; CP000254; ABD41200.1; -; Genomic_DNA.
DR   RefSeq; WP_011448469.1; NC_007796.1.
DR   AlphaFoldDB; Q2FP88; -.
DR   STRING; 323259.Mhun_1466; -.
DR   EnsemblBacteria; ABD41200; ABD41200; Mhun_1466.
DR   GeneID; 3922074; -.
DR   KEGG; mhu:Mhun_1466; -.
DR   eggNOG; arCOG04044; Archaea.
DR   HOGENOM; CLU_057069_2_2_2; -.
DR   InParanoid; Q2FP88; -.
DR   OrthoDB; 6329at2157; -.
DR   Proteomes; UP000001941; Chromosome.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   CDD; cd00958; DhnA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR   PANTHER; PTHR47916:SF3; FRUCTOSE-BISPHOSPHATE ALDOLASE_6-DEOXY-5-KETOFRUCTOSE 1-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ABD41200.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001941}.
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038992-1"
FT   ACT_SITE        206
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038992-1"
SQ   SEQUENCE   302 AA;  32489 MW;  07D2A1D14C0AA1A2 CRC64;
     MSKGFAVPLD VPKSEQDTYI RNLKTITHDS GRLMLFAGDQ KIEHLNDDFY GEGIHPDDHD
     PEHLFRIAAK AKIGCFATQL GLIAKYGADY PKIPYLIKIN SKTHLVPTAQ HEPFSNLINT
     IDQVVAFRKC SKLNILGIGY TIYLGSEYES AMLSAAAQAI FEAHQNGLVT VLWIYPRGKA
     VGNEKDPHLI AGAAGVAACL GSDFVKVNPP KGEGASSAEL IREATLAAGR TKVVCAGGSS
     VDAATFLTQL WEQIHVGGCS GNATGRNIHQ KPLDEAVRMC NAIYAITVDG ASVEDAIKIY
     HG
//
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