(data stored in ACNUC7421 zone)

SWISSPROT: Q3IJ23_PSEHT

ID   Q3IJ23_PSEHT            Unreviewed;       719 AA.
AC   Q3IJ23;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 101.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|SAAS:SAAS00256728};
GN   Name=fadB {ECO:0000313|EMBL:CAI85125.1};
GN   OrderedLocusNames=PSHAa0011 {ECO:0000313|EMBL:CAI85125.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85125.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85125.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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:SAAS00079501}.
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O. {ECO:0000256|SAAS:SAAS00656507}.
CC   -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CC       CoA. {ECO:0000256|SAAS:SAAS00079430}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH. {ECO:0000256|SAAS:SAAS00379695}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC       hydroxybutanoyl-CoA. {ECO:0000256|SAAS:SAAS00295821}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|SAAS:SAAS00649747}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
CC       chains (FadA). {ECO:0000256|SAAS:SAAS00079502}.
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:SAAS00649729}.
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DR   EMBL; CR954246; CAI85125.1; -; Genomic_DNA.
DR   RefSeq; WP_011326743.1; NC_007481.1.
DR   ProteinModelPortal; Q3IJ23; -.
DR   STRING; 326442.PSHAa0011; -.
DR   EnsemblBacteria; CAI85125; CAI85125; PSHAa0011.
DR   GeneID; 32565509; -.
DR   KEGG; pha:PSHAa0011; -.
DR   eggNOG; ENOG4105DYT; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   eggNOG; COG1250; LUCA.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; IDLCMIL; -.
DR   OrthoDB; POG091H00UW; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:InterPro.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:InterPro.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 2.
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_C-like.
DR   InterPro; IPR013328; 6PGD_dom_2.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR012799; FadB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IJ23.
DR   SWISS-2DPAGE; Q3IJ23.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Fatty acid metabolism {ECO:0000256|SAAS:SAAS00456821};
KW   Isomerase {ECO:0000256|SAAS:SAAS00656496,
KW   ECO:0000313|EMBL:CAI85125.1};
KW   Lipid degradation {ECO:0000256|SAAS:SAAS00051736};
KW   Lipid metabolism {ECO:0000256|SAAS:SAAS00456809};
KW   Lyase {ECO:0000256|SAAS:SAAS00656594, ECO:0000313|EMBL:CAI85125.1};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS00656592};
KW   NAD {ECO:0000256|SAAS:SAAS00830857};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00649305,
KW   ECO:0000313|EMBL:CAI85125.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   DOMAIN      317    495       3HCDH_N. {ECO:0000259|Pfam:PF02737}.
FT   DOMAIN      497    593       3HCDH. {ECO:0000259|Pfam:PF00725}.
FT   DOMAIN      628    689       3HCDH. {ECO:0000259|Pfam:PF00725}.
SQ   SEQUENCE   719 AA;  78276 MW;  4B555C0FDFA03B76 CRC64;
     MLYKSDSFEV SFIKENIAEF KFCATASVNT LSQQTLSDCA TALKQLAANT DIKGMIFTSD
     KEHFIIGADV FEFLPIFTRS EAELVTWIKE ATDVFDAIED LPFPTLSAVN GLALGGGCEW
     VLATDYRVAS ETAQMGLPEV TLGIMPGFGG TVRLPRIIGA DNAMMWITSG STNRAADALK
     VGAFDAVVSA DKLIESSVST LELAIAGKLD WQAKRNVKLQ PLKLNRVEQG MSFAMAEGMV
     MAKTKGHYPA PVMAVKTIKA AANCTRDEAM AIENANFAKL AGTPEVAAQI GIFLADQYIK
     GKSRKLAKQS DVEIKQAAVL GAGIMGGGIA YQSAYKGTPI IMKDIQQDAL DLGMGEASKL
     LGQKVKRGHM SMEKMLGTLS KIKPTLNDSD LQSADIIVEA VVENPKVKQA VLAELEKTMP
     EGTVLTSNTS TICIDLLAEA LDKPENFCGM HFFNPVPKMP LVEIIRGAKT SDKTINAVVD
     YALKLGKSPI VVNDCPGFFV NRVLFPYFAG FSKLVVEGAN FAKVDKVMEN VFGWPMGPAY
     LLDVVGIDTA FHCTGVMADG FPERMARADK DPVTIFANEK RFGQKNKAGF YKYETDRRGR
     LKKSHDETAI ELLKPITEAE KAFDKQEIID RCMIPMLNEV LLCLQEGIVA SPQEADMALV
     YGVGFPPFRG GAFRYLDQTG LANFVATADK YAHLGAIYQV SEQTRQWAEE GRVFYKVEG
//

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