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Fatty acid oxidation complex subunit alpha [Includes: 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35); Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8)]

 K1JYP9_9GAMM            Unreviewed;       715 AA.
K1JYP9;
28-NOV-2012, integrated into UniProtKB/TrEMBL.
28-NOV-2012, sequence version 1.
05-JUL-2017, entry version 35.
RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01621};
Includes:
RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01621};
EC=1.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01621};
Includes:
RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000256|HAMAP-Rule:MF_01621};
EC=4.2.1.17 {ECO:0000256|HAMAP-Rule:MF_01621};
EC=5.1.2.3 {ECO:0000256|HAMAP-Rule:MF_01621};
EC=5.3.3.8 {ECO:0000256|HAMAP-Rule:MF_01621};
Name=fadB {ECO:0000256|HAMAP-Rule:MF_01621};
ORFNames=HMPREF1170_00543 {ECO:0000313|EMBL:EKB24704.1};
Aeromonas veronii AMC35.
Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
Aeromonadaceae; Aeromonas.
NCBI_TaxID=1073385 {ECO:0000313|EMBL:EKB24704.1, ECO:0000313|Proteomes:UP000005385};
[1] {ECO:0000313|EMBL:EKB24704.1, ECO:0000313|Proteomes:UP000005385}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AMC35 {ECO:0000313|EMBL:EKB24704.1,
ECO:0000313|Proteomes:UP000005385};
The Broad Institute Genome Sequencing Platform;
Earl A., Ward D., Feldgarden M., Gevers D., Graf J., Tomasi A.,
Horneman A., Walker B., Young S.K., Zeng Q., Gargeya S.,
Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Aeromonas veronii AMC35.";
Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the aerobic and anaerobic degradation of
long-chain fatty acids via beta-oxidation cycle. Catalyzes the
formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA.
It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as
substrate. {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00079501}.
-!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CoA + H(2)O. {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00656507}.
-!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CoA. {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00079430}.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH. {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00379695}.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
hydroxybutanoyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00295821}.
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
{ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00649747}.
-!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
chains (FadA). {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00079502}.
-!- SIMILARITY: In the C-terminal section; belongs to the 3-
hydroxyacyl-CoA dehydrogenase family. {ECO:0000256|HAMAP-
Rule:MF_01621, ECO:0000256|SAAS:SAAS00556605}.
-!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
hydratase/isomerase family. {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00649729}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EKB24704.1}.
-----------------------------------------------------------------------
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EMBL; AGWW01000005; EKB24704.1; -; Genomic_DNA.
RefSeq; WP_005357367.1; NZ_JH815589.1.
EnsemblBacteria; EKB24704; EKB24704; HMPREF1170_00543.
PATRIC; fig|1073385.3.peg.548; -.
OrthoDB; POG091H00UW; -.
UniPathway; UPA00659; -.
Proteomes; UP000005385; Unassembled WGS sequence.
GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-HAMAP.
GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-HAMAP.
GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-HAMAP.
GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-HAMAP.
GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.1040.10; -; 2.
HAMAP; MF_01621; FadB; 1.
InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
InterPro; IPR006108; 3HC_DH_C.
InterPro; IPR008927; 6-PGluconate_DH_C-like.
InterPro; IPR013328; 6PGD_dom_2.
InterPro; IPR029045; ClpP/crotonase-like_dom.
InterPro; IPR001753; Crotonase_core_superfam.
InterPro; IPR012799; FadB.
InterPro; IPR016040; NAD(P)-bd_dom.
Pfam; PF00725; 3HCDH; 2.
Pfam; PF02737; 3HCDH_N; 1.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF48179; SSF48179; 2.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR02437; FadB; 1.
PROSITE; PS00067; 3HCDH; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000005385};
Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00456821};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00656496};
Lipid degradation {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00051736};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00051736, ECO:0000256|SAAS:SAAS00456821};
Lyase {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00656594};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00656592};
NAD {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00830857};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01621,
ECO:0000256|SAAS:SAAS00649305}.
DOMAIN 317 495 3HCDH_N. {ECO:0000259|Pfam:PF02737}.
DOMAIN 497 593 3HCDH. {ECO:0000259|Pfam:PF00725}.
DOMAIN 628 711 3HCDH. {ECO:0000259|Pfam:PF00725}.
NP_BIND 401 403 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
REGION 1 189 Enoyl-CoA hydratase/isomerase.
{ECO:0000256|HAMAP-Rule:MF_01621}.
REGION 311 715 3-hydroxyacyl-CoA dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_01621}.
ACT_SITE 451 451 For 3-hydroxyacyl-CoA dehydrogenase
activity. {ECO:0000256|HAMAP-
Rule:MF_01621}.
BINDING 296 296 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01621}.
BINDING 325 325 NAD; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01621}.
BINDING 344 344 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
BINDING 408 408 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
BINDING 430 430 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
BINDING 454 454 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
BINDING 501 501 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01621}.
BINDING 661 661 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01621}.
SITE 119 119 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_01621}.
SITE 139 139 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_01621}.
SEQUENCE 715 AA; 76464 MW; B69732541AAA8537 CRC64;
MIYQGETLSV SYLENGIAEL RFDAPGSVNK LDRATLLSLS EAIAALQQQA DLKGLILTSG
KDAFIVGADI TEFLELFDLP QEDLLGWLKK ANDIFNAIED LPVPTLSAIK GHALGGGCET
ILSTDFRLAD TSAKIGLPET KLGIMPGFGG TVRLPRVIGA DNALEWITTG KDYRADDALK
VGAIDAVVAP DALQSAALQM IKDAIAGKLD WQSRRAAKKA PLRLSKLEAM MSFTTAAGMV
AAVAGKHYPA PMTAVKTVEA AAGMGRDEAL VVEAQGFIKL AKTDVAKALV GIFLNDQHIK
ALAKKAAKQA SKATGHAAVL GAGIMGGGIA YQSASKGIPA VMKDINEKAL ALGMGEATKL
LNGQLEKGRI DGIKMGQVLS AITPTLSYDN VKHVDVVVEA VVENPKVKAA VLGEVEGIIG
EDAVLASNTS TIPISLLAKG LKRPQNFCGM HFFNPVHRMP LVEIIRGEQT SDETINRVVA
YAAAMGKSPV VVNDCPGFFV NRVLFPYFFG FNKLVADGAD FAAVDKVMEK EFGWPMGPAY
LLDVVGIDTG HHAGDVMAQG FPARMSKEGR TAIDVMYEVN RFGQKNGKGF YAYEQDKKGK
PKKVADATSY ELLAPIAKPK QDFDKDAIIA RMMIPMINEV VLCLEEGIVA TPAEADIALV
YGLGFPPFRG GVFRYLDTIG LDRYVAMADQ YADLGPLYRV SDRLREMAAQ GKTFY


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