GenomeNet

Database: UniProt
Entry: S9WDY9_CAMFR
LinkDB: S9WDY9_CAMFR
Original site: S9WDY9_CAMFR 
ID   S9WDY9_CAMFR            Unreviewed;       481 AA.
AC   S9WDY9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=2-hydroxyacyl-CoA lyase 1 isoform 3 {ECO:0000313|EMBL:EPY76592.1};
GN   ORFNames=CB1_001408009 {ECO:0000313|EMBL:EPY76592.1};
OS   Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY76592.1, ECO:0000313|Proteomes:UP000030684};
RN   [1] {ECO:0000313|EMBL:EPY76592.1, ECO:0000313|Proteomes:UP000030684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX   PubMed=23149746;
RG   Bactrian Camels Genome Sequencing and Analysis Consortium;
RA   Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA   Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA   Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA   Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA   Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA   Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA   Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA   Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA   Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA   Bayaer T., Li Y., Meng H.;
RT   "Genome sequences of wild and domestic bactrian camels.";
RL   Nat. Commun. 3:1202-1202(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxyoctadecanoyl-CoA = formyl-CoA + heptadecanal;
CC         Xref=Rhea:RHEA:55196, ChEBI:CHEBI:57376, ChEBI:CHEBI:74116,
CC         ChEBI:CHEBI:138631; Evidence={ECO:0000256|ARBA:ARBA00000194};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197;
CC         Evidence={ECO:0000256|ARBA:ARBA00000194};
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; KB017594; EPY76592.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9WDY9; -.
DR   Proteomes; UP000030684; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase 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   CDD; cd02004; TPP_BZL_OCoD_HPCL; 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; IPR045025; HACL1-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR   PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 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   Lyase {ECO:0000313|EMBL:EPY76592.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          17..85
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          98..225
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          294..377
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          454..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..481
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  52126 MW;  3CC79D5795162D7A CRC64;
     MESNVAEHSA GSEGQVSGAK VIAQALKTQG VRYMFGIVGI PVTEIALAAQ ELGIRYVGMR
     NEQAACYAAS VIGYLTGRYV ECCAPPPVCM AEASAVRLAA SIIRGARQPL VIVGKGAAYA
     RAEEGIRRLV EQCRLPFLPT PMGKGVIPDN HPNSVAAARS RALQSADVIV LFGARLNWIL
     HFGLPPRYQP DVKFIQVDIC AEELGNNVRP AVTLLGDINA VTEQLLEQFD KTPWQYPPES
     KWWKTLREKM KSNEAVSKEL ASQNSLPMNY YTVFYHVQDQ LPRDCFVVSE GANTMDIGRT
     VLQNYLPRHR LDAGTFGTMG VGLGFAIAAA IVAKDRSPGQ RVICVEGDSA FGFSGMEVET
     ICRYNLPIIL LVVNNNGIYQ GLSLADQLQN VKTPGPLPGL PSPTRDPGSH MATDFHKAIA
     KAARFSEDLA WSCQCPFCCT LLVKVARGQP SGSLFHESED SRLLPGEGPD AHSRGESDEA
     P
//
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