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
//