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Database: UniProt
Entry: A0A1Y4HRJ4_9BACT
LinkDB: A0A1Y4HRJ4_9BACT
Original site: A0A1Y4HRJ4_9BACT 
ID   A0A1Y4HRJ4_9BACT        Unreviewed;       334 AA.
AC   A0A1Y4HRJ4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Fructose-1,6-bisphosphate aldolase, class II {ECO:0000313|EMBL:OUP09360.1};
GN   ORFNames=B5F34_06850 {ECO:0000313|EMBL:OUP09360.1};
OS   Mediterranea sp. An20.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Mediterranea.
OX   NCBI_TaxID=1965586 {ECO:0000313|EMBL:OUP09360.1, ECO:0000313|Proteomes:UP000196631};
RN   [1] {ECO:0000313|Proteomes:UP000196631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An20 {ECO:0000313|Proteomes:UP000196631};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001359-3};
CC       Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC       provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUP09360.1}.
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DR   EMBL; NFJV01000009; OUP09360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4HRJ4; -.
DR   OrthoDB; 9803995at2; -.
DR   Proteomes; UP000196631; Unassembled WGS sequence.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   CDD; cd00947; TBP_aldolase_IIB; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR011289; Fruc_bis_ald_class-2.
DR   NCBIfam; TIGR00167; cbbA; 1.
DR   NCBIfam; TIGR01859; fruc_bis_ald; 1.
DR   PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001359-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196631};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001359-3}.
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
SQ   SEQUENCE   334 AA;  36695 MW;  4A0F1EDAB7FD7FE2 CRC64;
     MVNYKDLGLV NTREMFARAI KGGYAIPAFN FNNMEQLQAI IKASSEEKSP VILQVSKGAR
     NYANQTLLRY MAEGAVQYAK ELGCEHPEIV LHLDHGDSFE LCKSCVDMGF SSVMIDGSHL
     PYEENVALTK KVVEYAHQYD VTVEGELGVL AGVEDEVCAE HHTYTNPEEV IDFATRTGCD
     SLAISIGTSH GAYKFKPEQC HVDPATGRLV PPPLAFDVLD AVMEKLPGFP IVLHGSSSVP
     QEYVDMINKF GGNLEAAIGI PEDELRKAAK SAVCKINIDS DSRLAMTAAI RKVFAEKPAE
     FDPRKYLGPA RDEMEKLYKH KIINVLGSNG KLAQ
//
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