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Database: UniProt
Entry: A0A037ZNG4_9RHOB
LinkDB: A0A037ZNG4_9RHOB
Original site: A0A037ZNG4_9RHOB 
ID   A0A037ZNG4_9RHOB        Unreviewed;       608 AA.
AC   A0A037ZNG4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:KAJ57195.1};
GN   ORFNames=ACMU_01500 {ECO:0000313|EMBL:KAJ57195.1};
OS   Actibacterium mucosum KCTC 23349.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Actibacterium.
OX   NCBI_TaxID=1454373 {ECO:0000313|EMBL:KAJ57195.1, ECO:0000313|Proteomes:UP000026249};
RN   [1] {ECO:0000313|EMBL:KAJ57195.1, ECO:0000313|Proteomes:UP000026249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 23349 {ECO:0000313|EMBL:KAJ57195.1,
RC   ECO:0000313|Proteomes:UP000026249};
RA   Arahal D.R., Shao Z., Lai Q., Pujalte M.J.;
RT   "Draft Genome Sequence of Actibacterium mucosum KCTC 23349, a Marine
RT   Alphaproteobacterium with Complex Ionic Requirements Isolated from
RT   Mediterranean Seawater at Malvarrosa Beach, Valencia, Spain.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:KAJ57195.1}.
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DR   EMBL; JFKE01000001; KAJ57195.1; -; Genomic_DNA.
DR   RefSeq; WP_035255452.1; NZ_JFKE01000001.1.
DR   AlphaFoldDB; A0A037ZNG4; -.
DR   STRING; 1454373.ACMU_01500; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000026249; Unassembled WGS sequence.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR030817; Myo_inos_IolD.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR   PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KAJ57195.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026249};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          31..128
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          217..349
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          411..564
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   608 AA;  65014 MW;  50E527C19E921D2B CRC64;
     MNTIRLTAAQ ALVRYVSAQL NEDGEPFLAG CWAIFGHGNV AGLGEALYAH RDSFQTWRGH
     NEQTMAHAAI AYAKQSGRKR AMAVTSSIGP GATNMVTAAA LAHVNRIPVL FIPGDVFATR
     GPDPVLQQVE DFGDGTVSAN DCFRPVSRYF DRITRPEHLL TALPRAFATM TDPADCGPVT
     LAFCQDVQAE GYDWPVSFFE PNIWHQRRPR PDTGELARVT AAIEAAQNPV IVAGGGVHYS
     DACAELLEFA ERFQIPVVET QAGKSALPWD HPLNMGPVGV TGAASANTVC ETADLVLGVG
     TRFQDFTTGS WALFKNPART LISLNTAAYD AMKHGALPLM ADARVGLGEL TQALGDRRFT
     APSGALKTNW FAAVDPLTDA PEEGNALPTD QQVIGAVQRA SGPDTVVMCA AGTMPGELHK
     LWKAPRPGAY HMEYGFSCMG YEIAGAMGIK MAQPDRDVIC MIGDGSYMMA NSELATAVMM
     GIKFTMVITD NRGFGCINRL QMGTGGAEFN NLLDHAHHVN PSNIDFAAHA ASMGAAAVKV
     STIAELEEAL TRAADADGPF VVVIDTDPYP STPDGGTWWE VAVPEVSDRD EVTEARKGYE
     AALRARLN
//
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