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Database: UniProt
Entry: A0A1Q7HB33_9CHLR
LinkDB: A0A1Q7HB33_9CHLR
Original site: A0A1Q7HB33_9CHLR 
ID   A0A1Q7HB33_9CHLR        Unreviewed;       259 AA.
AC   A0A1Q7HB33;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase {ECO:0000313|EMBL:OLC48684.1};
GN   ORFNames=AUH82_02405 {ECO:0000313|EMBL:OLC48684.1};
OS   Chloroflexi bacterium 13_1_40CM_4_65_13.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1805074 {ECO:0000313|EMBL:OLC48684.1, ECO:0000313|Proteomes:UP000187427};
RN   [1] {ECO:0000313|EMBL:OLC48684.1, ECO:0000313|Proteomes:UP000187427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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:OLC48684.1}.
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DR   EMBL; MNFO01000020; OLC48684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7HB33; -.
DR   Proteomes; UP000187427; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR   PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          22..226
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   259 AA;  27770 MW;  503B66D0820DC651 CRC64;
     MTLRELWERG EPTLGGWCVI PSPFAAELMG RAGYDWICID TQHGLIGYDQ MLPMLQALSA
     TGTPAFVRVP WNQPSDIMKA LDAGAQGVIV PMVSSAEEAL RAVGACRFPP RGYRSWGPTR
     AALQVSGFGP ESASSAVVCV VMIETVEAMA NLDEILAVPG VDGVYVGPND LAVAHGLKPD
     ATAAAPEHRR LIETILEACR RHRLIAGIHC AGADTAIRWR EAGFRMLNVD NDALFLRGGA
     AHVLEALRGV KRDAARTGY
//
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