ID K6ZN33_9ALTE Unreviewed; 714 AA.
AC K6ZN33;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:AGH43936.1};
GN ORFNames=C427_1827 {ECO:0000313|EMBL:AGH43936.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH43936.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH43936.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH43936.1,
RC ECO:0000313|Proteomes:UP000011864};
RX PubMed=23640379;
RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL Genome Announc. 1:E00199-13(2013).
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};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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DR EMBL; CP003837; AGH43936.1; -; Genomic_DNA.
DR AlphaFoldDB; K6ZN33; -.
DR STRING; 1129794.C427_1827; -.
DR KEGG; gps:C427_1827; -.
DR PATRIC; fig|1129794.4.peg.1811; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_3_6; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000011864; Chromosome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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 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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR PANTHER; PTHR23309:SF9; PEROXISOMAL BIFUNCTIONAL ENZYME; 1.
DR Pfam; PF00725; 3HCDH; 2.
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; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000011864}.
FT DOMAIN 310..486
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 491..584
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 620..709
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 714 AA; 77348 MW; 3ED07F295E31F5F6 CRC64;
MSQVESKTVN SDAVNYELIE TPSANKVAVL WMQNPPVNAL SKSVRVGLIK HLNAAIADES
VQVIVISSKQ SLFSGGADIS EFSGGDLEPN LPAVLDVIEN SPKPVVAVLN GPAFGGGLEV
ALSCHYRLTF ASNKVGLPEV NLGILPGAGG TQRLPRLAGV QQALDMIVSG RPVAADKLPG
VFDVVVDSPE TLLTSALAFC EKVIADGSKV RKTCDVKIDV SSAPKELFAQ YRQGLATKAR
GFFAPERCIQ AVEASVELPF AQGLIREGEL FMECMRSKEA RAQQHFFFAE RAASHVKDFD
KETPVRDIKQ VGIIGAGTMG GGIAMNFANA GIPVIMLELK QDALDKGLAL IRKNYENSAK
KGKLTAQQVE DRMGLLTGST EYAALCNVDL VIEAVFEKMS VKQEVFKALD AVCKPGAILA
SNTSTLDIDE IGEATKRPED VIGLHFFSPA NVMKLLEVVK TSKTSPEVIK TTMKMAKKIN
KVAVLVGVCF GFVGNRMIEG YGREANRMML EGGTPEHIDK VIYDFGLPMG PFTMGDMAGQ
DIGAFVRESR REFIKHDPSY CILADKLVEQ GRVGLKVGKG VYLYEAGSRK PIPDPSVLEL
AKQVAADLGV AQRDISDQEI IERIIFPMIN EGALILEEGI AAKSSDIDVI YVYGYGFPVY
RGGPMQYADE IGLKTVYDAM CKYRDELGEH GKNWFEPAPL LKKLAEQGKR FSDL
//
