ID B9LP36_HALLT Unreviewed; 582 AA.
AC B9LP36;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:ACM57124.1};
GN OrderedLocusNames=Hlac_1536 {ECO:0000313|EMBL:ACM57124.1};
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM57124.1, ECO:0000313|Proteomes:UP000000740};
RN [1] {ECO:0000313|EMBL:ACM57124.1, ECO:0000313|Proteomes:UP000000740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC {ECO:0000313|Proteomes:UP000000740};
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(2016).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001365; ACM57124.1; -; Genomic_DNA.
DR RefSeq; WP_015910264.1; NC_012029.1.
DR AlphaFoldDB; B9LP36; -.
DR GeneID; 7401466; -.
DR KEGG; hla:Hlac_1536; -.
DR eggNOG; arCOG01998; Archaea.
DR HOGENOM; CLU_013748_3_1_2; -.
DR Proteomes; UP000000740; Chromosome 1.
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:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic 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:UP000000740};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 19..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 205..339
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 416..565
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 171..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 60337 MW; 2F8E11E5B7A37BA9 CRC64;
MDTDESQSGT DPSAVDAPTV AEAVVDCMLD RGIDVAFGIP GKQTLPLNRA LGERDARFVV
ARHETAVTHQ AWGYAETSDP GAMAASIVVP GPGDMNAMNG LKNALNDCVP LLHLAVETER
EVRGGDGIHE TPPETYDTVV KENVLVDSPA GAVPAVAEAI RVAREHPQGP VRVGIPKDVL
ASRTPQPAIG DREPAAPPDP PADAVDRAAD LLAGAGSPVI LAGGGVRRAG ASDSLRAIAE
RLDAPVVTTY KGKGTLPETH PLSAGVLCGG SSTELRDLLA DADRGLVVGS DLDAVATASW
SVSLPDSLIH VTLDGDDIGF GYEADLGIVA DADRFLQALG DRLGDEEEEM LASEPAGSAS
HPESPGAARA DAVRSADRER FAALADERSA NDPLRSVEVL REVREALPAE AVVTADAGGF
RLWTLVSFPA AGPSRYVNPG SWATMGTGLP SAIGAKLANP DRDVVALTGD GGLMMCVHEL
HTLAAEGIDV TVVAFTNDDY AIISEEASRS YDLPAGAYGW AETAIDLVAV ASGMGVRAER
VTDRDAVGEA LTSALAHDGP ALIEVATDPD EPQASEWMTR ER
//
