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Database: UniProt
Entry: Q30RJ2_SULDN
LinkDB: Q30RJ2_SULDN
Original site: Q30RJ2_SULDN 
ID   Q30RJ2_SULDN            Unreviewed;       310 AA.
AC   Q30RJ2;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=HpcH/HpaI aldolase {ECO:0000313|EMBL:ABB44389.1};
GN   OrderedLocusNames=Suden_1111 {ECO:0000313|EMBL:ABB44389.1};
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=326298 {ECO:0000313|EMBL:ABB44389.1, ECO:0000313|Proteomes:UP000002714};
RN   [1] {ECO:0000313|EMBL:ABB44389.1, ECO:0000313|Proteomes:UP000002714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251 {ECO:0000313|Proteomes:UP000002714};
RX   PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP000153; ABB44389.1; -; Genomic_DNA.
DR   RefSeq; WP_011372741.1; NC_007575.1.
DR   AlphaFoldDB; Q30RJ2; -.
DR   STRING; 326298.Suden_1111; -.
DR   KEGG; tdn:Suden_1111; -.
DR   eggNOG; COG2301; Bacteria.
DR   HOGENOM; CLU_044864_0_1_7; -.
DR   Proteomes; UP000002714; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR32308:SF1; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002714}.
FT   DOMAIN          38..248
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   310 AA;  35371 MW;  DA449C2ADA1C2F8E CRC64;
     MINNLQEIIE AYESRDLKAL NLLAVPTCRT LNKRADFRSL LMLSCNNLKH LTKIDTLEAD
     AIILNLEDGV SKVDKPFALV LCAIFLSYYK RCDKKLIVRV NALNEGGYDE IAYLKNFMPD
     AIRVPKIRDK KEVESVCELL DEKIELHLSI ETKEAWNSML ELRVDKNVTT FYLGILDIFA
     DMKLSQTLIS RENPVVLYML SHFLISSKSI GVKPVSFVYQ EFKKLPEFEM WLSLEKSMGY
     DAKGCLSPTQ ASIANRVFTS SEAEIKRAEI IVKLFELKQE EGISGFEDKE FGFIDEPIYK
     GALATLNKNV
//
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