ID Q1QTM2_CHRSD Unreviewed; 545 AA.
AC Q1QTM2;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Thiamine pyrophosphate enzyme-like TPP binding region {ECO:0000313|EMBL:ABE60186.1};
GN OrderedLocusNames=Csal_2840 {ECO:0000313|EMBL:ABE60186.1};
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE60186.1, ECO:0000313|Proteomes:UP000000239};
RN [1] {ECO:0000313|EMBL:ABE60186.1, ECO:0000313|Proteomes:UP000000239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11
RC {ECO:0000313|Proteomes:UP000000239};
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000285; ABE60186.1; -; Genomic_DNA.
DR RefSeq; WP_011508132.1; NC_007963.1.
DR AlphaFoldDB; Q1QTM2; -.
DR STRING; 290398.Csal_2840; -.
DR KEGG; csa:Csal_2840; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_6; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000000239; 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 GO; GO:0019752; P:carboxylic acid 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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:UP000000239};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 15..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..336
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 545 AA; 57469 MW; C7A76C4B8E52A5EA CRC64;
MTHETSASSS TQISCAEALV RLLRDRYAVD TVFGIPGVHT VPLYRGLEAG GLRHVTPRHE
QGAGFMADGY ARASGKPGVC FIITGPGMTN IATAMGQALA DSVPMLVISS VNRRDTLGRG
QGRLHELPSQ QNVLAGVSRF SHTLLDPSAL PEVLARAFAM FQSARPGPVH IEIPIDLFEA
PIDLPDTASP TRLYRAGAHP EGIALAAEWL RQAQAPLVLL GGGCAEASKA ARTLVEHLDA
PTVTTINAKG VLGRGHPLDL GANATWPEVR ALARDADVIL AVGTELGETD YDVVFDDGFT
LTGRLIRIDL EAEQLVRNQA TALGLVSDAQ AALEALAAHF PSPLARQGAA RVRAVHEALA
LPQRPDMAPF VPLYTALDKA LPEAILVGDS TAPVYAGNHL VERAAPRRYF NASTGYGTLG
YGLPAALGAQ LAAPGTPVVA LVGDGGAMFT LSELATAVDE GLPVVVVLWN NSGYEEIRRY
MDVHGVARIG VDPTPPDFQC LADGFGLASH RVESPIALDL ALSKVSRTSP TLIEIDAERW
QAALD
//
