(data stored in SCRATCH zone)

SWISSPROT: A4ATJ1_MARSH

ID   A4ATJ1_MARSH            Unreviewed;       355 AA.
AC   A4ATJ1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:EAR00761.1};
GN   OrderedLocusNames=FB2170_16791 {ECO:0000313|EMBL:EAR00761.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00761.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00761.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|SAAS:SAAS00836928};
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|SAAS:SAAS00836930}.
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DR   EMBL; CP002157; EAR00761.1; -; Genomic_DNA.
DR   RefSeq; WP_013304564.1; NC_014472.1.
DR   STRING; 313603.FB2170_16791; -.
DR   EnsemblBacteria; EAR00761; EAR00761; FB2170_16791.
DR   KEGG; fbc:FB2170_16791; -.
DR   eggNOG; ENOG4105D2N; Bacteria.
DR   eggNOG; COG0191; LUCA.
DR   HOGENOM; HOG000227794; -.
DR   KO; K01624; -.
DR   OMA; ELCKDCI; -.
DR   OrthoDB; 827430at2; -.
DR   BioCyc; MSP313603:G1GNS-135-MONOMER; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   CDD; cd00946; FBP_aldolase_IIA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR006411; Fruct_bisP_bact.
DR   PANTHER; PTHR30559; PTHR30559; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   TIGRFAMs; TIGR00167; cbbA; 1.
DR   TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATJ1.
DR   SWISS-2DPAGE; A4ATJ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Lyase {ECO:0000256|SAAS:SAAS00132197};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3,
KW   ECO:0000256|SAAS:SAAS00132199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001359-3, ECO:0000256|SAAS:SAAS00132210}.
FT   REGION      262    264       Dihydroxyacetone phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR001359-2}.
FT   REGION      283    286       Dihydroxyacetone phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR001359-2}.
FT   ACT_SITE    106    106       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001359-1}.
FT   METAL       107    107       Zinc 1; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001359-3}.
FT   METAL       141    141       Zinc 2. {ECO:0000256|PIRSR:PIRSR001359-
FT                                3}.
FT   METAL       171    171       Zinc 2. {ECO:0000256|PIRSR:PIRSR001359-
FT                                3}.
FT   METAL       223    223       Zinc 1; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001359-3}.
FT   METAL       261    261       Zinc 1; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001359-3}.
FT   BINDING     224    224       Dihydroxyacetone phosphate; via amide
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR001359-
FT                                2}.
SQ   SEQUENCE   355 AA;  38837 MW;  E51A5CB45C4E1AC0 CRC64;
     MAHNIKPGVA TGDQVQEIFN YAKEKGFALP AVNVIGSDTI NGVLETAAAL NAPVIIQFSN
     GGAQFNAGKG LSNDGQNAAV QGAVAGAKHV HQLAEAYGAS VILHTDHCAK KLLPWIDGLL
     DASEKHYAET GKSLFSSHMI DLSEEPIEEN IEICKGYLER MSKMDMTLEI ELGITGGEED
     GVDNSDVDDS KLYTQPEEVA YAYEELSKVS PKFTIAAAFG NVHGVYKPGN VKLTPKILKN
     SQEYISKKYG VEHNHIDFVF HGGSGSTVEE IREAIGYGVI KMNIDTDLQY AFLAGVRDYV
     QDKKDYLQGQ IGNPSGSDEP NKKYYDPRVW LREGEKSFIE RLKKAFDDLN NVNTL
//

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