ID S4RFA8_PETMA Unreviewed; 581 AA.
AC S4RFA8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=2-hydroxyacyl-CoA lyase 1 {ECO:0000313|Ensembl:ENSPMAP00000003890.1};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000003890.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000003890.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; S4RFA8; -.
DR STRING; 7757.ENSPMAP00000003890; -.
DR Ensembl; ENSPMAT00000003906.1; ENSPMAP00000003890.1; ENSPMAG00000003546.1.
DR GeneTree; ENSGT00940000156802; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR OMA; YMGMIGM; -.
DR Proteomes; UP000245300; Unplaced.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000245300};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 18..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 402..559
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 62568 MW; 37EA497876E512F2 CRC64;
PREPPEMSAQ DETGEQLTGA QLIAEALLEQ GIEFMFGVVG VPIIEVALAA QQVGIKYIGM
RNEQAACYAA SAVGYLTNRP GICLVVSGPG LIHALGGMAN ANVNCWPVLV LGGSSDQDQE
AMGAFQEFPQ VESCRLYSKF SARPSSLQSI PGIVEKAVRT SIYGRPGACY IDIPGNMVNA
TITRESVKFL PRCLPPPVSM ADPQSVAAAA ATLRNAKRPL VIVGKGAGYA RAEHSVRRLV
DDFALPFLPT PMGKGVLPDD HPRCVAAARS RALQHADVVL LLGARLNWML HFGLPPRFRH
DVKIIQVDVC AEELGNNVKP SSPLLGDVTA VTMQIVDQLG ISRWTFPADS EWWTFLKEKI
DANSRISKAM VSDQTLPMNY YTVFHHVAEL LPRDAIVVSE GANTMDIGRT MLNNALPRHR
LDAGTFGTMG VGLGYAIAAA MVVKQQDPPP KVVCVEGDSA FGFSGMEVET MVRYKLPVVV
LVVNNNGIYA GLDEDTWALL SQAGDAASVV PPTSLLPGAR YEQVMSAFGG RGFLARTPKE
LREALQASLA EPSLPCLINV LISPSADRKK QEFSWLTRSN L
//
