ID B1XZ85_LEPCP Unreviewed; 545 AA.
AC B1XZ85;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Vinylacetyl-CoA Delta-isomerase {ECO:0000313|EMBL:ACB35255.1};
DE EC=5.3.3.3 {ECO:0000313|EMBL:ACB35255.1};
GN OrderedLocusNames=Lcho_2993 {ECO:0000313|EMBL:ACB35255.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB35255.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB35255.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001013; ACB35255.1; -; Genomic_DNA.
DR RefSeq; WP_012348009.1; NC_010524.1.
DR AlphaFoldDB; B1XZ85; -.
DR STRING; 395495.Lcho_2993; -.
DR KEGG; lch:Lcho_2993; -.
DR eggNOG; COG2368; Bacteria.
DR HOGENOM; CLU_023920_1_0_4; -.
DR OrthoDB; 7233724at2; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0050393; F:vinylacetyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.3140.10; 4-hydroxybutyryl-coa dehydratase, domain 1; 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; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR PANTHER; PTHR36117; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR36117:SF3; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR Pfam; PF03241; HpaB; 1.
DR Pfam; PF11794; HpaB_N; 1.
DR PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|PIRSR:PIRSR000331-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Isomerase {ECO:0000313|EMBL:ACB35255.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT DOMAIN 17..284
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 293..494
FT /note="HpaB/PvcC/4-BUDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03241"
FT BINDING 203
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ SEQUENCE 545 AA; 58979 MW; 9335A4E970755163 CRC64;
MHAAPPTRTA ATAGLMTAVD YRESLRRLRP VVYVDGQRIE SVADAPSLQP GINALGVTYD
LAHDPAMARL MTARHTRSGR TVNRMLHVNE SAGDLLDKLE AVRLLCQETG CAQRYLAHDA
LNAIGQVSAR IDDARGSTEH RARFEAYLQR VQTEDLALGI AMTDAKGDRS RRPHQQANPD
THVHVVERKP QGIVISGTKA IVTGAPYMHE FLVMPGRNMS REDADFAVCC AVPVDAPGIT
IVARPAGRPG EKVEHGAPLF SRRYGQSTGV VIFDRVFVPW ERVFYAGEWE HSGTLTYHYA
THHRHSCIGA RAGFGDLLIG AGALMCEANG FDPGQTSSLR EPMVELIKIT EGFFACGVAA
SVYGTADQHS GTFMPEPVFA NIGKLLLATQ IYDMHRLAHE VSGGLIVALP GPDEDHNPAT
AATLAEVLRA NPAVPYDKRI EVARFVEDLT ASYQAGWYSV ISLHGGGSPA AMKQEIWRNY
PLGNKVDLVE RLLDRGVLAP TEGGDTRAIT RNRQPGRCCD SGCTQPGQAV MVALPVSTRD
DVAGA
//
