GenomeNet

Database: UniProt
Entry: A0A0W7TWV0_9GAMM
LinkDB: A0A0W7TWV0_9GAMM
Original site: A0A0W7TWV0_9GAMM 
ID   A0A0W7TWV0_9GAMM        Unreviewed;       715 AA.
AC   A0A0W7TWV0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   03-JUL-2019, entry version 33.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01621};
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=4.2.1.17 {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=5.1.2.3 {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=5.3.3.8 {ECO:0000256|HAMAP-Rule:MF_01621};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=1.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01621};
GN   Name=fadB {ECO:0000256|HAMAP-Rule:MF_01621,
GN   ECO:0000313|EMBL:KUE78308.1};
GN   ORFNames=ATO46_11510 {ECO:0000313|EMBL:KUE78308.1};
OS   Aeromonas schubertii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=652 {ECO:0000313|EMBL:KUE78308.1, ECO:0000313|Proteomes:UP000054876};
RN   [1] {ECO:0000313|EMBL:KUE78308.1, ECO:0000313|Proteomes:UP000054876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE78308.1,
RC   ECO:0000313|Proteomes:UP000054876};
RA   Liu L., Li Q., Zhang F., Shi B.;
RT   "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the aerobic and anaerobic degradation of
CC       long-chain fatty acids via beta-oxidation cycle. Catalyzes the
CC       formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA.
CC       It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as
CC       substrate. {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00051718}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-hydroxybutanoyl-CoA = (3R)-hydroxybutanoyl-CoA;
CC         Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC         EC=5.1.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01621,
CC         ECO:0000256|SAAS:SAAS01121794};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC         EC=5.3.3.8; Evidence={ECO:0000256|HAMAP-Rule:MF_01621,
CC         ECO:0000256|SAAS:SAAS01132199};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+)
CC         + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01621, ECO:0000256|SAAS:SAAS01123908};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01621, ECO:0000256|SAAS:SAAS01133165};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC         EC=5.3.3.8; Evidence={ECO:0000256|HAMAP-Rule:MF_01621,
CC         ECO:0000256|SAAS:SAAS01132197};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-hydroxyacyl-CoA = a (3E)-enoyl-CoA +
CC         H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01621, ECO:0000256|SAAS:SAAS01123900};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00324886}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
CC       chains (FadA). {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00051733}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-
CC       hydroxyacyl-CoA dehydrogenase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01621, ECO:0000256|SAAS:SAAS00556605}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00568097}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KUE78308.1}.
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; LPUO01000056; KUE78308.1; -; Genomic_DNA.
DR   RefSeq; WP_050665369.1; NZ_LPUO01000056.1.
DR   EnsemblBacteria; KUE78308; KUE78308; ATO46_11510.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000054876; Unassembled WGS sequence.
DR   GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01621; FadB; 1.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
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; IPR012799; FadB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR02437; FadB; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054876};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00324839};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00324648};
KW   Lipid degradation {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00256736};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00324863};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00999128};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00999134};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00830857};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00324627}.
FT   DOMAIN      317    495       3HCDH_N. {ECO:0000259|Pfam:PF02737}.
FT   DOMAIN      497    593       3HCDH. {ECO:0000259|Pfam:PF00725}.
FT   DOMAIN      628    710       3HCDH. {ECO:0000259|Pfam:PF00725}.
FT   NP_BIND     401    403       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   REGION        1    189       Enoyl-CoA hydratase/isomerase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   REGION      311    715       3-hydroxyacyl-CoA dehydrogenase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   ACT_SITE    451    451       For 3-hydroxyacyl-CoA dehydrogenase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   BINDING     296    296       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   BINDING     325    325       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     344    344       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     408    408       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     430    430       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     454    454       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     501    501       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   BINDING     661    661       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   SITE        119    119       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   SITE        139    139       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
SQ   SEQUENCE   715 AA;  76206 MW;  24AD6CC7E84CC5B9 CRC64;
     MIYQGETLSV RYLEDGIAEL RFDAPGSVNK LDRATLLSLS EAISALQQQT DLRGLILTSG
     KDAFIVGADI TEFLELFALP DEQLLGWLKK ANDIFNAIED LPVPTLSAIK GHALGGGCET
     ILSTDFRLAD STAKIGLPET KLGIMPGFGG TVRLPRVIGA DNALEWITTG KDYRADDALK
     VGAVDAVVAP AALTAAAIQM IKDAADGKLD WQGRRAAKKA PLRLSRLEAM MSFSTAAGMV
     AAVAGKHYPA PMAAVKTVET AAGMGRDEAL AAEAATFIKL AKTDVAKALV GIFLNDQHIK
     ALAKQSAKKA SKATNHAAVL GAGIMGGGIA YQSASKGIPA VMKDINEKAL ALGMGEATKL
     LNGQLEKGRI DGIKMGQVLS AITPTLSYDS VKGVDLVVEA VVENPKVKAA VLGEVEAVLG
     DDAVLASNTS TIPISLLAKG LKRPENFCGM HFFNPVHRMP LVEIIRGEQT SDETIDRVVA
     YAAAMGKSPV VVNDCPGFFV NRVLFPYFFG FNKLVADGAD FAAVDKVMEK EFGWPMGPAY
     LLDVVGIDTG HHAGDVMAQG FPTRMTKDGR TAIDVMYEAS RFGQKNGKGF YAYEADKKGK
     PKKVADAAAY ELLAPIAKPQ QAFDKETIIA RMMIPMINEV VLCLEEGIIA TPAEADIALV
     YGLGFPPFRG GVFRYLDTMG LDRYVAMADQ FADLGPLYRV SNQLREMAAQ GKTFY
//
DBGET integrated database retrieval system