ID V2TZG9_9GAMM Unreviewed; 717 AA.
AC V2TZG9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 ORFNames=P253_02447 {ECO:0000313|EMBL:ESK47338.1};
OS Acinetobacter indicus CIP 110367.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1341679 {ECO:0000313|EMBL:ESK47338.1, ECO:0000313|Proteomes:UP000018415};
RN [1] {ECO:0000313|EMBL:ESK47338.1, ECO:0000313|Proteomes:UP000018415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110367 {ECO:0000313|EMBL:ESK47338.1,
RC ECO:0000313|Proteomes:UP000018415};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter indicus CIP 110367.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the aerobic and anaerobic degradation of long-
CC chain fatty acids via beta-oxidation cycle. Catalyzes the formation of
CC 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use
CC D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
CC {ECO:0000256|HAMAP-Rule:MF_01621}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-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 -!- 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00023693, ECO:0000256|HAMAP-
CC Rule:MF_01621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-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};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC 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};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005, ECO:0000256|HAMAP-Rule:MF_01621}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC (FadA). {ECO:0000256|HAMAP-Rule:MF_01621}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_01621}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750,
CC ECO:0000256|HAMAP-Rule:MF_01621}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01621}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK47338.1}.
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DR EMBL; AYET01000006; ESK47338.1; -; Genomic_DNA.
DR RefSeq; WP_016659666.1; NZ_KI530756.1.
DR AlphaFoldDB; V2TZG9; -.
DR PATRIC; fig|1341679.3.peg.2380; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_3_6; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000018415; 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:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.10.1040.50; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; 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 NCBIfam; TIGR02437; FadB; 1.
DR PANTHER; PTHR43612:SF8; FATTY ACID OXIDATION COMPLEX SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00067; 3HCDH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_01621}; Isomerase {ECO:0000256|HAMAP-Rule:MF_01621};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW Rule:MF_01621}; Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01621};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01621};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01621};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01621};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01621}; Reference proteome {ECO:0000313|Proteomes:UP000018415}.
FT DOMAIN 318..496
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 498..593
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 1..190
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT REGION 313..717
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT ACT_SITE 452
FT /note="For 3-hydroxyacyl-CoA dehydrogenase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT BINDING 326
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT BINDING 345
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT BINDING 402..404
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT BINDING 409
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT BINDING 431
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT BINDING 455
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT BINDING 502
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT SITE 120
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
FT SITE 140
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01621"
SQ SEQUENCE 717 AA; 77813 MW; E0DF865086431AF8 CRC64;
MIHAGNAITV QMLSDGIAEF RFDLQGESVN KFNRATIEDF KAAIDAVKAN SEIKGLVVTS
GKSTFIVGAD ITEFGENFAQ GEQAIVEWAL PVHDIFNAFE DLDIPKVAAI NGMALGGGFE
MCLVCDYRVM SEQAQVGLPE IKLGIFPGFG GTVRLSRLIG IDNAVEWMAM ANPKKPAAAL
KDGAVDAVVA ADKLTEAAVD LAKQAAAGRL DWKAKRQEKL DPVKLNPLEQ MMAFNTAKGA
VLAKANPAQY PAPKLMLDSL QAGASLPRND ALKAEAEGFA KAAVTPQAGA LIGLFINDQV
VKKTSKKYEK GAHPVNQAAV LGAGIMGGGI AYQAASKGTP IIMKDIGNPQ LALGMSEANK
LLTKQVERKK MTPAKMGETL ARIRPTLSYD EFKEVDIVIE AVTENPKVKG IVLAETEKNV
RDNTIIASNT STISITRLAE NLQRPENFVG MHFFNPVHMM PLVEVIRGEK TSPEAIATTV
VLAQKMGKTP IVVNDCPGFL VNRVLFPYFG AFDLLLKDGA DFQQVDKVME KFGWPMGPAY
LIDVVGIDTG VHGAEVMAEG FPDRMKPDYK GSIQVMYENK RLGQKNDVGF YKYELDRKGK
KAKVVDPTAY ELVASVATTE KREFDAQEII DRMMLAFCNE TVRCLEDNIV ATPSEADMAM
IMGVGFPPFR GGPCRYIDQT GVAEYVALCD KYAHLGKAYE APQMLRDMAA NNKKFYG
//
