ID A5U0P8_MYCTA Unreviewed; 720 AA.
AC A5U0P8;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Fatty oxidation complex subunit alpha {ECO:0000313|EMBL:ABQ72598.1};
GN Name=fadB {ECO:0000313|EMBL:ABQ72598.1};
GN OrderedLocusNames=MRA_0868 {ECO:0000313|EMBL:ABQ72598.1};
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947 {ECO:0000313|EMBL:ABQ72598.1, ECO:0000313|Proteomes:UP000001988};
RN [1] {ECO:0000313|EMBL:ABQ72598.1, ECO:0000313|Proteomes:UP000001988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra {ECO:0000313|Proteomes:UP000001988};
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(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: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000611; ABQ72598.1; -; Genomic_DNA.
DR RefSeq; WP_003404426.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U0P8; -.
DR SMR; A5U0P8; -.
DR KEGG; mra:MRA_0868; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_15_3_11; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001988; Chromosome.
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:UP000001988}.
FT DOMAIN 328..505
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 508..607
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 720 AA; 76104 MW; 52CB1865400F3BE5 CRC64;
MPDNTIQWDK DADGIVTLTM DDPSGSTNVM NEAYIESMGK AVDRLVAEKD SITGVVVASA
KKTFFAGGDV KTMIQARPED AGDVFNTVET IKRQLRTLET LGKPVVAAIN GAALGGGLEI
ALACHHRIAA DVKGSQLGLP EVTLGLLPGG GGVTRTVRMF GIQNAFVSVL AQGTRFKPAK
AKEIGLVDEL VATVEELVPA AKAWIKEELK ANPDGAGVQP WDKKGYKMPG GTPSSPGLAA
ILPSFPSNLR KQLKGAPMPA PRAILAAAVE GAQVDFDTAS RIESRYFASL VTGQVAKNMM
QAFFFDLQAI NAGGSRPEGI GKTPIKRIGV LGAGMMGAGI AYVSAKAGYE VVLKDVSLEA
AAKGKGYSEK LEAKALERGR TTQERSDALL ARITPTADAA DFKGVDFVIE AVFENQELKH
KVFGEIEDIV EPNAILGSNT STLPITGLAT GVKRQEDFIG IHFFSPVDKM PLVEIIKGEK
TSDEALARVF DYTLAIGKTP IVVNDSRGFF TSRVIGTFVN EALAMLGEGV EPASIEQAGS
QAGYPAPPLQ LSDELNLELM HKIAVATRKG VEDAGGTYQP HPAEAVVEKM IELGRSGRLK
GAGFYEYADG KRSGLWPGLR ETFKSGSSQP PLQDMIDRML FAEALETQKC LDEGVLTSTA
DANIGSIMGI GFPPWTGGSA QFIVGYSGPA GTGKAAFVAR ARELAAAYGD RFLPPESLLS
//
