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Database: UniProt
Entry: D1PZ42_9BACT
LinkDB: D1PZ42_9BACT
Original site: D1PZ42_9BACT 
ID   D1PZ42_9BACT            Unreviewed;       337 AA.
AC   D1PZ42;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Fructose-1,6-bisphosphate aldolase, class II {ECO:0000313|EMBL:EFA43276.1};
DE            EC=4.1.2.13 {ECO:0000313|EMBL:EFA43276.1};
GN   Name=fba {ECO:0000313|EMBL:EFA43276.1};
GN   ORFNames=HMPREF0645_2227 {ECO:0000313|EMBL:EFA43276.1};
OS   Hallella bergensis DSM 17361.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hallella.
OX   NCBI_TaxID=585502 {ECO:0000313|EMBL:EFA43276.1, ECO:0000313|Proteomes:UP000003160};
RN   [1] {ECO:0000313|EMBL:EFA43276.1, ECO:0000313|Proteomes:UP000003160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17361 {ECO:0000313|EMBL:EFA43276.1,
RC   ECO:0000313|Proteomes:UP000003160};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (OCT-2009) 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:EFA43276.1}.
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DR   EMBL; ACKS01000082; EFA43276.1; -; Genomic_DNA.
DR   RefSeq; WP_007174330.1; NZ_GG704781.1.
DR   AlphaFoldDB; D1PZ42; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_040088_0_0_10; -.
DR   OrthoDB; 9803995at2; -.
DR   Proteomes; UP000003160; Unassembled WGS sequence.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
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:0000313|EMBL:EFA43276.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003160};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         96
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         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         191
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         235
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   337 AA;  37071 MW;  05638C4AD3C977C1 CRC64;
     MAVSYKDLGL VNTRDMFKRA VSGGYAIPAF NFNNLEQLQA IITASSELKS PVILQVSKGA
     RNYANATLLR YMAEGAVEYA KELGCKHPEI VLHLDHGDTF ELCKDCVDMG FSSVMIDGSS
     LPYEENVELA KKVVDYAHKY DVTVEAELGV LAGVEDDVVA EESHYTKPEE VIDFSKRTGC
     DSLAISIGTS HGAYKFTPEQ CTRDPKTGRL VPPPLAFDIL AEIEKKLPGF PIVLHGSSSV
     PQEYVDIINK FGGHLPNAVG IPEEQLRQAA KSAVCKVNID SDSRLAYTAG VRETLSEHPE
     YFDPRQYGKV ARNYMIDLYK SKITNVLGSN NKLAQLD
//
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