ID A9ISH9_BORPD Unreviewed; 705 AA.
AC A9ISH9;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Fatty oxidation complex alpha subunit {ECO:0000313|EMBL:CAP43304.1};
DE EC=1.1.1.35 {ECO:0000313|EMBL:CAP43304.1};
GN Name=fadB1 {ECO:0000313|EMBL:CAP43304.1};
GN OrderedLocusNames=Bpet2962 {ECO:0000313|EMBL:CAP43304.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP43304.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP43304.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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DR EMBL; AM902716; CAP43304.1; -; Genomic_DNA.
DR AlphaFoldDB; A9ISH9; -.
DR STRING; 94624.Bpet2962; -.
DR KEGG; bpt:Bpet2962; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
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.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:CAP43304.1};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 303..478
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 483..576
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 612..697
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 705 AA; 75138 MW; 36114E738683BAB2 CRC64;
MAESAPHGAV ASQRHDGILV LTIDHPPVNA LSADVRRGLA DAIQAAQSDA AIQAIVLVGA
GRNFIAGADI REFGKPPQPP ALPDVCNAIE ASAKPVIAAL HGAALGGGLE IALAAHYRVA
LPGARLGLPE VNLGLLPGAG GTQRTPRLAG AAAALDLMLS GRHAGTDEAL SWGLIDRIGA
GADAQAAGLD YARELLAQGA GPRRTRDAAG LADRPAAQAA IDAARAQVQS RQRGLFSPAK
IVDAVQAALD QPFDEGLRTE RALFLQCLDS PQRAALVHAF FAERETAKAP ETRQARPRPL
ERLGVIGGGT MGAGIAVAML DAGLPVVMVE QNDEALARGR ARVEQVYDLL VKKGRLDAAG
KAERMARYTG ATRYEALADA DLIVEAVFED MDVKLAVFAE LDRIAKPGAV LATNTSYLDI
NRIAAATSRP GDVLGLHFFS PANIMKLLEI VVGANSAPDT VATGFELARR LRKTPVRAGV
CDGFIGNRIL AVYRQAADLM LEDGASPYQI DDAVRAFGYP MGPYQVADLA GGDIGWATRK
RRAATRDPRL RYVQIPDRLC ERGWFGQKTG RGYYLYPDGA RTGTPDPEVL AIIDAERQRA
GVTPRQFTQE DILRRYLAAM VNEAANVLRE GIALRPLDID VVFLSGYGFP RFRGGPLHYA
DQVGLPRILA DIREFAQEDP HFWQPSPLLV ELADSGRGFD SLNRA
//
