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Database: UniProt
Entry: K8PHY8_9BRAD
LinkDB: K8PHY8_9BRAD
Original site: K8PHY8_9BRAD 
ID   K8PHY8_9BRAD            Unreviewed;       695 AA.
AC   K8PHY8;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKS41156.1};
GN   ORFNames=HMPREF9695_00248 {ECO:0000313|EMBL:EKS41156.1};
OS   Afipia broomeae ATCC 49717.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=883078 {ECO:0000313|EMBL:EKS41156.1, ECO:0000313|Proteomes:UP000001096};
RN   [1] {ECO:0000313|EMBL:EKS41156.1, ECO:0000313|Proteomes:UP000001096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49717 {ECO:0000313|EMBL:EKS41156.1,
RC   ECO:0000313|Proteomes:UP000001096};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Afipia broomeae ATCC 49717.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00023693};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKS41156.1}.
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DR   EMBL; AGWX01000001; EKS41156.1; -; Genomic_DNA.
DR   RefSeq; WP_006018950.1; NZ_KB375282.1.
DR   AlphaFoldDB; K8PHY8; -.
DR   PATRIC; fig|883078.3.peg.258; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_16_3_5; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001096; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.1040.50; -; 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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00725; 3HCDH; 1.
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   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001096}.
FT   DOMAIN          324..497
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          501..596
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   695 AA;  75239 MW;  0F3CD384123B0F28 CRC64;
     MDSRIMDVLK DRVLELGPEP QAGPYRNFKL TRDSDGIAWL LFDREGTSAN TLSASVLEEF
     ETVIAALEQD RPAGIVIRSA KPSGFIAGAD VNEFRGVTDP REVESQMARA HAVVDRLEAL
     KVPSVAVIHG FCLGGGLEVA LACNTRIAID NARFGFPEVM LGLHPGLGGT ARFTHLVSPL
     EAMTMMLTGK TIDARKAKSL GLADAVTQER HVRNAVKDAI FGRLRPHRQG LLARAMNLGP
     VRGLLANRMR GEAAKTAPKD HYPAPYALIG LWEKHGGDRK AMLAAEQVSF ANLMVTPTAQ
     NLIRVFFLRE QMKKLADGRN TVKHVHVIGA GAMGGDIAAW CAYQGLRVTL ADMKAEPIAG
     AVKRASDLFG KIIRKKADLR DALDRLMPDM TGEGVRNADL IIEAVPEKLE LKQKVYAGLE
     PVMKAGAILA TNTSSIPLQD LRTTLTHPER LLGLHFFNPV SRLQLVEVVS HDTVDPHALA
     TALKFVGAID RLPLPVKSSP GFLVNRALTP YMLEAMVMLD EKVDKAVIDA AAEKFGMPMG
     PIELADQVGL DICLAVGDML RSKFGEAALP PAPDWLRDKV KKGELGRKTG KGFYEWKDGK
     AVKLPSPVQP TEEMIDRLIL PMSNVCVACL REGIVENGDV VDGAMIFGTG YAPFRGGPLN
     YARTRGAANV VAALKALEAK FGGRFKPDAG WDTFA
//
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