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Database: UniProt
Entry: F7RWA6_9GAMM
LinkDB: F7RWA6_9GAMM
Original site: F7RWA6_9GAMM 
ID   F7RWA6_9GAMM            Unreviewed;       713 AA.
AC   F7RWA6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   08-MAY-2019, entry version 48.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|SAAS:SAAS00051741};
GN   ORFNames=A28LD_0527 {ECO:0000313|EMBL:EGN76039.1};
OS   Idiomarina sp. A28L.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN76039.1, ECO:0000313|Proteomes:UP000053031};
RN   [1] {ECO:0000313|EMBL:EGN76039.1, ECO:0000313|Proteomes:UP000053031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A28L {ECO:0000313|EMBL:EGN76039.1,
RC   ECO:0000313|Proteomes:UP000053031};
RX   PubMed=21742887; DOI=10.1128/JB.05648-11;
RA   Gupta H.K., Singh A., Sharma R.;
RT   "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong
RT   Lake, India.";
RL   J. Bacteriol. 193:5875-5876(2011).
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|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|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|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;
CC         Evidence={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;
CC         Evidence={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|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;
CC         Evidence={ECO:0000256|SAAS:SAAS01123900};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|SAAS:SAAS00324886}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
CC       chains (FadA). {ECO:0000256|SAAS:SAAS00051733}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|RuleBase:RU003707}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-
CC       hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|SAAS:SAAS00556605}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000256|SAAS:SAAS00556608}.
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:EGN76039.1}.
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DR   EMBL; AFPO01000007; EGN76039.1; -; Genomic_DNA.
DR   RefSeq; WP_007419512.1; NZ_AFPO01000007.1.
DR   STRING; 1036674.A28LD_0527; -.
DR   EnsemblBacteria; EGN76039; EGN76039; A28LD_0527.
DR   PATRIC; fig|1036674.4.peg.518; -.
DR   eggNOG; ENOG4105DYT; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   eggNOG; COG1250; LUCA.
DR   OrthoDB; 977512at2; -.
DR   BioCyc; ISP1036674:G11F1-1096-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000053031; 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-EC.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
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; 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; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000053031};
KW   Fatty acid metabolism {ECO:0000256|SAAS:SAAS00324839};
KW   Isomerase {ECO:0000256|SAAS:SAAS00442736};
KW   Lipid degradation {ECO:0000256|SAAS:SAAS00256736};
KW   Lipid metabolism {ECO:0000256|SAAS:SAAS00324863};
KW   Lyase {ECO:0000256|SAAS:SAAS00999128};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS00999134};
KW   NAD {ECO:0000256|SAAS:SAAS00830857};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00331296};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053031}.
FT   DOMAIN      316    494       3HCDH_N. {ECO:0000259|Pfam:PF02737}.
FT   DOMAIN      496    592       3HCDH. {ECO:0000259|Pfam:PF00725}.
FT   DOMAIN      624    688       3HCDH. {ECO:0000259|Pfam:PF00725}.
SQ   SEQUENCE   713 AA;  77021 MW;  68034A577DE23165 CRC64;
     MIYKGDNLHV DFIEPGIAEI TFDAPGSVNK FDEKTLTEFS EALDALTGNN DLRGVLVRSA
     KPTFIVGADI TEFLTLFADL EKTKTWVHKA SRVFDKLEDL PVPSIAAVNG FALGGGCEAI
     LACDYRIVDE TAVIGLPEVK LGLIPGFGGT VRLPRVIGPD NALEAITTGM NHKPEKALAV
     GLVDAVTSSD RLKEGALSML RDAIAGELDW KAKRQPKLEA LKANDTEKLM SFSTAKGMIW
     AKAGKHYPSP HAALEVVERG AGEGREAALN IENELFVKLT QTDAARAQVG IFLADQLVKG
     KSKKVAKSAT KKISRAGVLG AGIMGGGIAY QSASRGVPVV MKDIRRDALD LGLNEASKIL
     GKALERGKIS QKLVAKTLTS ITPTLNNSEL ADVDIIVEAV VENPKIKASV LAEVEKVVAK
     DAIITSNTST ISIDKLAESL EDPSRFCGMH FFNPVHKMPL VEIIRGKHTS DETIAAVTAY
     ALQMGKTAIV VNDCPGFLVN RVLFPYFAGF SKLLDDDIDF TGIDKVMEKE FGWPMGPAYL
     CDVVGMDTAD HATNVMAEGF PTRMARDDNG AIAKLAAAER YGQKNGKGFY EYSVDKRGRP
     QKVVNPDVYD IIGKKSASAE KEEIIARCMI PMVNEMVRCV EEGIVDSAEE ADIALIYGLG
     FPPFRGGAFR YLETLGLEKF VELADKYADL GEIYQVTDGL REKAKTGGTY FKS
//
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