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Database: UniProt
Entry: G5ZWQ7_9PROT
LinkDB: G5ZWQ7_9PROT
Original site: G5ZWQ7_9PROT 
ID   G5ZWQ7_9PROT            Unreviewed;       554 AA.
AC   G5ZWQ7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:EHI49490.1};
GN   ORFNames=HIMB100_00004510 {ECO:0000313|EMBL:EHI49490.1};
OS   SAR116 cluster alpha proteobacterium HIMB100.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX   NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI49490.1, ECO:0000313|Proteomes:UP000004261};
RN   [1] {ECO:0000313|EMBL:EHI49490.1, ECO:0000313|Proteomes:UP000004261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX   PubMed=22675578; DOI=10.4056/sigs.1854551;
RA   Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA   D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA   Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA   Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA   Kyrpides N.C., Rappe M.S.;
RT   "Draft genome sequence of strain HIMB100, a cultured representative of the
RT   SAR116 clade of marine Alphaproteobacteria.";
RL   Stand. Genomic Sci. 5:269-278(2011).
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:EHI49490.1}.
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DR   EMBL; AFXB01000004; EHI49490.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5ZWQ7; -.
DR   STRING; 909943.HIMB100_00004510; -.
DR   PATRIC; fig|909943.3.peg.461; -.
DR   eggNOG; COG0028; Bacteria.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000004261; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd00568; TPP_enzymes; 1.
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; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EHI49490.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004261};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..120
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          192..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          388..524
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   554 AA;  58634 MW;  B816D7CE8B0DCB3F CRC64;
     MSTGHVTGGQ LLVSCLDTLG AKTSFGVPGE SYLAVLDALY DADIRFVLCR QEGAASFAAA
     AWGKLTGAPG ICFVTRGPGA TNASIGVHTA MQDSSPMILF VGQIGVDHKE REAFQEVDYR
     AFFGSMAKWA TEIDNVDRIP EILARAWRVA LSGRPGPVVI ALPEDMLTAQ TTAQPCRPVT
     VAEAGVDQTQ MDHVAALLAD ADRPLVLAGG GGWAPQGRQD LQAFCEREHL PMAAIFRYHD
     IVDNHSPCYI GDAGVGMAPH VSDAIAEADV ILAVNARFGE ATTKAWTLLD VPNPKQHIIQ
     THASDRELGK IYQPEIALHA GPNQVSSTLT HLQLDTTKSA QRKDWLAGLK ASYEASLQPA
     AQNSPVDMAA VMSWLQDNLA DDVIITNGAG NFALWPNKVF SYGPKQTLLA PQSGAMGYGL
     PAAIAASLAC PERQVICFAG DGDIQMGLAE LGTAVQSGAR PIILLLNNGS YGTIRMHQER
     DYPDRISGTT LINPDFAAVA KAYGMAGIKV SSTEEFASAF DAVSQSATGG IIELDIAVEA
     ITPRTTLSAL RAGR
//
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