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Database: UniProt
Entry: A0A0M2VIK7_9GAMM
LinkDB: A0A0M2VIK7_9GAMM
Original site: A0A0M2VIK7_9GAMM 
ID   A0A0M2VIK7_9GAMM        Unreviewed;       717 AA.
AC   A0A0M2VIK7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-MAY-2019, entry version 26.
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:KKO49400.1};
GN   ORFNames=VT06_06080 {ECO:0000313|EMBL:KKO49400.1};
OS   Arsukibacterium sp. MJ3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Arsukibacterium.
OX   NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO49400.1, ECO:0000313|Proteomes:UP000034895};
RN   [1] {ECO:0000313|EMBL:KKO49400.1, ECO:0000313|Proteomes:UP000034895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ3 {ECO:0000313|EMBL:KKO49400.1,
RC   ECO:0000313|Proteomes:UP000034895};
RA   Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J.,
RA   Stougaard P., Glaring M.A.;
RT   "Draft genome sequences of two protease-producing strains of
RT   Arsukibacterium isolated from two cold and alkaline environments.";
RL   Submitted (MAR-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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01621}.
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:KKO49400.1}.
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DR   EMBL; LAHP01000006; KKO49400.1; -; Genomic_DNA.
DR   RefSeq; WP_046553401.1; NZ_LAHP01000006.1.
DR   EnsemblBacteria; KKO49400; KKO49400; VT06_06080.
DR   PATRIC; fig|1632859.4.peg.1254; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000034895; 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; 1.
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:UP000034895};
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, ECO:0000313|EMBL:KKO49400.1};
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, ECO:0000256|SAAS:SAAS00999128,
KW   ECO:0000313|EMBL:KKO49400.1};
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, ECO:0000313|EMBL:KKO49400.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034895}.
FT   DOMAIN      316    495       3HCDH_N. {ECO:0000259|Pfam:PF02737}.
FT   DOMAIN      497    593       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    717       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   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   717 AA;  77127 MW;  052B6084693820B8 CRC64;
     MIYQSDTISV EYSKPGIVRF TFAAAGSVNK FDQQTLTDCK KALELLHADS NLKGVIFTSS
     KDTFIVGADI TEFLTTFQRP ESELIPWIKQ ASDIFDLCED LPVPTVAAIK GFALGGGCEW
     TLACDYRVAD TSTRIGLPEV KLGLMPGFGG TVRLPRIIGA DNAMEWITTG KDHSADQAQK
     VGLIDAVVAP EKLLDAALSV LEDAIAGSLN WQKKRAVKLQ PLKLNKIEAT MCFSTAKGMV
     FATAGKHYPA PMAAVQTIEA AATLDRAGAM ALENAGFAKL AKTDAATAQV GLFLNDQLIK
     SKAKKAGKIA TKTIKKAAVL GAGIMGGGIA YQSALKGVPV IMKDIADKAL ALGMGEATKL
     LSKQVERKKL DIAGMAKVIA SITPTLSNEL VKDVDIVVEA VVENPKIKGA VLKEVEGLIS
     DDAILTSNTS TISINALAKN LSRPENFCGM HFFNPVHRMP LVEVIRGKDT SDETIAAVVA
     FAARMGKSPI VVNDCPGFFV NRVLFPYFAG FSKLVLDGAD FAQVDKVMEK QFGWPMGPAY
     LLDVVGLDTA FHCTDVMAEG FPSRMAKLEK DPVAAMYNAE RYGQKNGLGF YAYSKDAKGK
     PKKDIDPKSV ALLAEIASTR QDFTPDEIIA RVMVPMINET IRCLEEGIVQ SAAEADMGLI
     FGLGFPPFRG GPLRYVDTIG LKHFVALADK YAHLGEIYQV TDKTRAMADN GQRFFPV
//
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