ID A0A139WVZ0_9CYAN Unreviewed; 287 AA.
AC A0A139WVZ0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:KYC36601.1};
GN ORFNames=WA1_43735 {ECO:0000313|EMBL:KYC36601.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC36601.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC36601.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC36601.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC {ECO:0000256|ARBA:ARBA00005086}.
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:KYC36601.1}.
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DR EMBL; ANNX02000047; KYC36601.1; -; Genomic_DNA.
DR RefSeq; WP_017744624.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139WVZ0; -.
DR STRING; 128403.WA1_43735; -.
DR OrthoDB; 9771883at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
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; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925}.
FT DOMAIN 6..184
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 187..283
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT SITE 141
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 287 AA; 31873 MW; 083D8AE544E8A960 CRC64;
MKIQVVGVVG AGVMGIGVAQ NLSQTGHQVI LVDISEDILE NAKKEIRNNV RFQGFFQKNQ
QAESPDNILH RIKFSTNYKF LESAEFVIEN ATEKWDIKKG IYAQLDAICP EKTVFAANTS
AISITRIASV TKRADKVIGM HFMNPVPMKP MVEMIRGYHT SDDAIATAKE LLAQMGKECI
LVNDSPGFVS NRVLMLTINE AIFLLQDRVA SVEEVDKIFT SCFGHKMGPL ETADLIGLDT
ILFSIEVLYE SFNDSKYRPC PLLKKMVDAG LYGRKNGQGF YTYSGAT
//
