ID U9WBF4_9CYAN Unreviewed; 604 AA.
AC U9WBF4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Isovaleryl-dehydrogenase {ECO:0000313|EMBL:ESA37461.1};
GN ORFNames=N836_02815 {ECO:0000313|EMBL:ESA37461.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA37461.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA37461.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA37461.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:ESA37461.1}.
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DR EMBL; AWNH01000024; ESA37461.1; -; Genomic_DNA.
DR RefSeq; WP_023071762.1; NZ_AWNH01000024.1.
DR AlphaFoldDB; U9WBF4; -.
DR STRING; 1385935.N836_02815; -.
DR PATRIC; fig|1385935.3.peg.1732; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 3666321at2; -.
DR Proteomes; UP000017515; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd00567; ACAD; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000017515}.
FT DOMAIN 31..112
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 124..222
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 234..380
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 604 AA; 67595 MW; 7528003CA11EF7B0 CRC64;
MKSLKQYWVA EALERSLGSP FTPENPLSFQ HTATLDEQEV FPEAEIKGLY DWGLQHYYIP
TDCGGKFTSF EEFVAFVRVL SRRDLNTAIA FTTMFWSFLT WMAGTETQKQ QLARFMKDDY
GTMCLAYSER EHGSDLVGGS LVGEKVPGGY RLTGEKWPIN RATRSGITFV LARTDKAGGN
RGLSLFMLDK RALDPTSFGN NPKIKTHGIR GADMSGIYFE DCFVPDEMLL GKEGQGLELA
LKGFQITRAL CAAFSQGSAD TCLRTTLNFA LNRQLYGKTV WDMPHPRRVL VNGFLDILAC
DCVNIAAARG FHVAPRQFSV WSAVDKYFVP VTLEKMQQDI SVVLGARFYM RDEHDYGVFQ
KMLRDSSIIS VFDGSSVVNL HSLILQRRQL AKARSRRKPK DLVALQARLR NSFDLTTELP
AFAPSQLDLI ARGTDDVSQG LESALATLEA LGKPLDIDAN VLDCLKQQYQ QFLQVLDEQD
EAIADGAFEH GHDQSFESFE EAKGYCYIHA AAACLHMWLH NRSQLGDFFA QGKWLVLCAD
RLLAQLTPEQ PAIPLAYYET VAEELLRLHR ADKMLSIVPF QLASRTNSVS ASAPIKSPAP
ILQV
//
