ID G4RCE6_PELHB Unreviewed; 552 AA.
AC G4RCE6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=TPP-requiring enzyme co-localized with fatty acid metabolic genes {ECO:0000313|EMBL:AEQ53740.1};
GN OrderedLocusNames=KKY_3758 {ECO:0000313|EMBL:AEQ53740.1};
OS Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS B2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Devosiaceae; Pelagibacterium.
OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ53740.1, ECO:0000313|Proteomes:UP000008850};
RN [1] {ECO:0000313|EMBL:AEQ53740.1, ECO:0000313|Proteomes:UP000008850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC {ECO:0000313|Proteomes:UP000008850};
RX PubMed=22156395; DOI=10.1128/JB.06343-11;
RA Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL J. Bacteriol. 194:197-198(2012).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP003075; AEQ53740.1; -; Genomic_DNA.
DR RefSeq; WP_014132884.1; NC_016078.1.
DR AlphaFoldDB; G4RCE6; -.
DR STRING; 1082931.KKY_3758; -.
DR KEGG; phl:KKY_3758; -.
DR PATRIC; fig|1082931.4.peg.3708; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_5; -.
DR Proteomes; UP000008850; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 Reference proteome {ECO:0000313|Proteomes:UP000008850};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..106
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 552 AA; 58986 MW; 20D63BE4B31BDDDF CRC64;
MTTLKTYDVL AKAFVQEDVD TCFALLGDAN MNWGTTLSTL GVRMIYVRHE HCAVASAMAY
ARKSGKTGVA TVTCGPGLTQ LMTALPAAVR ANLPLVIFAG EAPLKSGWYN QGIDQAPFIT
ATGAIYRSLH HIERMPEAVR DAFLDARMAG KPVVLGVPFD LQDRDWPGEM ALPAPSATLI
PDVGPVPPHP DDIARAADRV ARAKKIVVMA GMGAVSAGAG QACRKLAEKC DGLLATTLPA
RGLFCDDPYC LGVAGGFSTE AGRQLMAEAD LIIAVGSILA HHNADGGKLF GSAHVLQIDL
DPVTVSQGRV AAHSHVRADA RLGVEALNEK IEARLNHWRN EETARFIRET PPDSEHFPAA
GNLLDPRAVV AALETHLPPD WEMVNSSGHC SYFFAQMPSR PQHRFLTIRE FGAIGNGISF
AMGVAAARPD DTVVLFDGDG SLMMHIQEIE TIARHGLNIL ICILNDGAYG SEIHKLRAEG
LSDEGAVFGR SDFASIARGF GIGGETITDL SALPSLIEGF RRRGGAAIWD FPISDQVISP
VIRRAHPPVT YA
//
