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Database: UniProt
Entry: Q9HLD7_THEAC
LinkDB: Q9HLD7_THEAC
Original site: Q9HLD7_THEAC 
ID   Q9HLD7_THEAC            Unreviewed;       658 AA.
AC   Q9HLD7;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=L-3-hydroxyacyl-CoA dehydrogenase related protein {ECO:0000313|EMBL:CAC11436.1};
GN   OrderedLocusNames=Ta0291 {ECO:0000313|EMBL:CAC11436.1};
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075 {ECO:0000313|EMBL:CAC11436.1, ECO:0000313|Proteomes:UP000001024};
RN   [1] {ECO:0000313|EMBL:CAC11436.1, ECO:0000313|Proteomes:UP000001024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165
RC   {ECO:0000313|Proteomes:UP000001024};
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.L., Koretke K.K., Volker C.,
RA   Mewes H.W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
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DR   EMBL; AL445063; CAC11436.1; -; Genomic_DNA.
DR   RefSeq; WP_010900720.1; NC_002578.1.
DR   AlphaFoldDB; Q9HLD7; -.
DR   STRING; 273075.gene:9571508; -.
DR   PaxDb; 273075-Ta0291; -.
DR   EnsemblBacteria; CAC11436; CAC11436; CAC11436.
DR   GeneID; 1455916; -.
DR   KEGG; tac:Ta0291; -.
DR   eggNOG; arCOG00249; Archaea.
DR   HOGENOM; CLU_010448_2_0_2; -.
DR   InParanoid; Q9HLD7; -.
DR   OrthoDB; 39812at2157; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001024; Chromosome.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR   PANTHER; PTHR23309:SF9; PEROXISOMAL BIFUNCTIONAL ENZYME; 1.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001024}.
FT   DOMAIN          5..183
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          186..280
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          303..369
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   658 AA;  72229 MW;  DE80E3FABBA2ACF8 CRC64;
     MEINKVTVIG SGIMGHGIAE VIALAGIDVN IEDISNEVLD KAKASINSSL DRLVSSGKLK
     NKDEVLSRIH YFTDIPSSVK DADLVIEAVP EVLDIKKSVF DQLDKSTKDS AILATNTSNI
     RLTEIAEGIK KKGKVVGMHF FNPPVVLKLV EVIRSQYTED EVFETVYEFS KRIGKTPIKV
     YKDTPGFVVN RINAPESLYF CLVIDNNLAK PEEVDRFARS QGLPMGPYEL MDYVGIDTVY
     HSLQYYAKEL SPDYSKCQVY TKLFNEKKLG LKTGEGFYKW VNGKAQIPEA KPTKAVELMD
     IFALEINEAV KIIEDGVASP DDIETGVKLG MNRPFGPITV AKGLTNAEVK AKLEALYQKF
     SVEVFKPAKS IAEGKLKTVI SMQVALSKAE EKKEAASAYI SSSDPVIMET KGRIAILRIN
     NTKNNLINAA VMDGLEKALT DLWNNREISV IVLTGNGPVF SAGAQLDSFF SSTFDFMEFS
     RRGERVFKLL SEIPKVTIAE LKGYTLGGGF EMALACDIRV ATEDVQIGFP EVTLGLVPGW
     GGTQRLSRTA GQSRAAYYIL TGERFTGKEA YEMGIVAKIF SKDTIDSETL NLAQNIADKV
     APISAALAKR LVLRSTNTSL DDGLEMEAIS MGLLYGTEDL KEGISAFLGK RKPNYQGK
//
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